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Biochemistry Flashcards

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7813415564carbohydrateProvides energy0
7813415565pHmeasures the acidity and base of a substance1
7813415566compoundA pure substance made of two or more elements CHEMICALLY combined.2
7813415567moleculeA neutral group of atoms joined together by covalent bonds; smallest unit of a compound joined together3
7813415568cellBasic unit of life4
7813415569calorieAmount of energy needed to raise temperature 1 gram of water 1 degree C'; A unit of heat used to measure the energy your body uses and the energy it receives from food5
7813415570energyAbility to do work or cause change6
7813415571elementA pure substance made of only one kind of atom7
7813415572phosphate bonda high-energy chemical bond that is especially important between the 2nd and 3rd phosphate groups in an ATP molecule8
7813415573starchA storage polysaccharide in plants consisting entirely of glucose.9
7813415574organicCarbon-containing10
7813415575inorganicDoes not contain carbon; Not formed from living things or the remains of living things11
7813415576synthesisCombining of small molecules or substances into larger, more complex ones; A+B=AB12
7813415577proteinA macromolecule that contains the principal components of organisms: carbon, hydrogen, oxygen, and nitrogen; performs a variety of structural and regulatory functions for cells.13
7813415578energy storagecarbohydrates and lipids14
7813415579structural support15
7813415580dehydration reactionA chemical reaction in which two molecules covalently bond to each other with the removal of a water molecule.16
7813415581biological moleculechemical compounds that provide physical structure and bring about movement, energy use, and other cellular functions in a living organism17
7813415582active siteRegion of an enzyme into which a particular substrate fits.18
7813415583activation energythe minimum amount of energy required to start a chemical reaction19
7813415584saturated fatA lipid made from fatty acids that have no double bonds between carbon atoms; A fat that is solid at room temperature and found in animal fats, lards, and dairy products.20
7813415585unsaturated fatA lipid made from fatty acids that have at least one double bond between carbon atoms; A fat that is liquid at room temperature and found in vegetable oils, nuts, and seeds.21
7813415586fatty acidBuilding Blocks of Lipids; substances produced when fats are digested; simple forms of fat that supply energy fuel for most of the body's cells; unbranched carbon chains that make up most lipids22
7813415587steroidsA type of lipid characterized by a carbon skeleton consisting of four rings with various functional groups attached.23
7813415588exothermic reactionA reaction that releases energy in the form of heat24
7813415589endothermic reactionA reaction that ABSORBS energy in the form of heat25
7813415590fructase-ase suffix Most enzymes end in "-ase" suffix, but not all enzymes. Some enzymes were named prior to the adoption of this process; "ose" turns to "ase" after decomposition reactions; structural -- what gives a macromolecule its shape [chitin]26
7813415591"ose"used in biochemistry to form the names of sugars27
7813415592chemical structureThe way atoms in a compound are bonded it represents the structure of a compound.28
7813415593covalent bondA chemical bond that involves sharing a pair of electrons between atoms in a molecule29
7813415594ionic bondFormed when one or more electrons are transferred from one atom to another30
7813415595polar moleculeMolecule with an unequal distribution of charge, resulting in the molecule having a positive end and a negative end31
7813415596hydrogen bondA type of weak chemical bond formed when the slightly positive hydrogen atom of a polar covalent bond in one molecule is attracted to the slightly negative atom of a polar covalent bond in another molecule.32
7813415597biochemicalThe changing of organic matter into other chemical forms such as fuels.33
7813415598macromoleculeA very large organic molecule composed of many smaller molecules; a molecule containing a very large number of atoms, such as a protein, nucleic acid, or synthetic polymer.34
7813415599catalyst(chemistry) a substance that initiates or accelerates a chemical reaction without itself being affected35
7813415600enzymeA type of protein that speeds up a chemical reaction in a living thing36
7813415601substrateA specific reactant acted upon by an enzyme; reactant of an enzyme-catalyzed reaction37
7813415602polymerA long molecule consisting of many similar or identical monomers linked together.38
7813415603monomersmall chemical unit that makes up a polymer39
7813415604polysaccharideA polymer of thousands of simple sugars formed by dehydration synthesis; Carbohydrates that are made up of more than two monosaccharides40
7813415605disaccharideA double sugar molecule made of two monosaccharides bonded together through dehydration synthesis.41
7813415606monosacchridesingle sugar molecule42
7813415607fructoseA monosaccharide found predominantly in fruit and honey43
7813415608celluloseA large polysaccharide composed of many glucose monomers linked into cable-like fibrils that provide structural support in plant cell walls.44
7813415609lipidEnergy-rich organic compounds, such as fats, oils, and waxes, that are made of carbon, hydrogen, and oxygen.45
7813415610nucleotideA building block of DNA, consisting of a five-carbon sugar covalently bonded to a nitrogenous base and a phosphate group.46
7813415611amino acidBuilding blocks of protein47
7813415612nucleic acid(biochemistry) any of various macromolecules composed of nucleotid chains that are vital constituents of all living cells48
7813415613peptideThe chemical bond that forms between the carboxyl group of one amino acid and the amino group of another amino acid49
7813415614triglycerideComposed of three molecules of fatty acids joined to one molecule of glycerol50
7813415615dehydration synthesisA chemical reaction in which two molecules covalently bond to each other with the removal of a water molecule.51
7813415616glycerolA three-carbon alcohol to which fatty acids are covalently bonded to make fats and oils.52
7813415617phospholipidA molecule that is a constituent of the inner bilayer of biological membranes, having a polar, hydrophilic head and a nonpolar, hydrophobic tail.53
7813415618maltosea 12-carbon sugar that is formed by the union of two glucose units (a disaccharide)54
7813415619cyclicoccurring in cycles; regularly repeated55
7813415620chitina fibrous substance consisting of polysaccharides56
7813415621hydrolysisA chemical reaction that breaks bonds between two molecules by the addition of water; functions in disassembly of polymers to monomers.57
7813415622sucroseA disaccharide made of glucose + fructose; Table sugar58
7813415623glycogenA highly branched polymer of glucose containing thousands of subunits; functions as a compact store of glucose molecules in liver and muscle fibers59
7813415624hexosescarbohydrates with six carbon atoms60
7813415625enzyme activitythe ability of an enzyme to do work and is mainly dependent on substrate concentration61
7813415626enzyme substrate complexA temporary complex formed when an enzyme binds to its substrate molecule(s).62
7813415627polymerizationAn organic reaction in which many small units are joined together to form a long chain63

Biochemistry Flashcards

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7281873291ElementPure substance composed of all the same type of atom.0
7281873292AtomThe smallest particle of an element that retains all the properties of that element.1
7281877691ProtonsPositively charged subatomic particles found in the nucleus of an atom.2
7281883010NeutronsSubatomic particles that have no charge.3
7281885841ElectronsSmall, negatively charged subatomic particles that move about the nucleus at very high speeds and are located in the orbitals.4
7281894930CompoundA substance of atoms or two or more elements in a fixed proportion.5
7281898750MoleculeThe simplest unit of a compound that retains all the properties of that substance.6
7281902965IonAn atom or molecule that has lost or gained one or more electrons resulting in an atom or molecule with an electrical charge.7
7281910552EnergyThe ability to do work.8
7281912520ReactantsThe elements or compounds that enter into a chemical reaction.9
7281915423ProductsThe elements or compounds produced by a chemical reaction.10
7281919195Activation energyThe amount of energy required to start a reaction.11
7281922563CohesionThe attraction between molecules of the same substance.12
7281926951AdhesionThe attraction between molecules of different substances.13
7281930656SolutionA homogeneous mixture of the molecules of two or more substances.14
7281935787AcidA solution in which the number of hydronium ions exceeds the number of hydroxide ions.15
7281942319BaseA solution in which the number of hydroxide ions exceeds the number of hydronium ions.16
7281949835pH scaleA scale used to compare the relative concentrations of hydronium ions and hydroxide ions in a solution.17
7281956976BufferA chemical substance that can neutralize small amounts of either an acid or a base in a solution to prevent sudden changes in pH.18
7281974700Adenosine Triphosphate (ATP)The energy-carrying molecule of the cell that is energy rich.19
7281977370CarbohydrateOrganic compounds composed of carbon, hydrogen and oxygen in a 1:2:1 ratio.20
7281982323ProteinsOrganic compounds composed of carbon, hydrogen, oxygen and nitrogen.21
7281989177Amino AcidsThe monomers that are the building blocks of proteins.22
7281992708EnzymeA protein that acts as a biological catalyst to speed up the chemical reactions within the cell.23
7281998268SubstrateThe substance, or reactant, of an enzymatic reaction.24
7282002119Active SiteAn indentation, pocket or groove on the surface of an enzyme into which a particular substrate can fit.25
7282007431LipidLarge, nonpolar organic molecules composed of fatty acids and glycerol molecules that do not dissolve in water.26
7282017297Nucleic AcidsVery large and complex organic molecules that store and transfer important information in the cell.27
7282027537Deoxyribonucleic Acid (DNA)The type of nucleic acid that contains the information that determines the characteristics of an organism and directs it cellular activities.28
7282036068Ribonucleic Acid (RNA)The type of nucleic acid that transfers information about protein synthesis from the nucleus to the ribosomes.29
7282042686NucleotideThe repeating monomers that compose nucleic acids.30

Biochemistry Flashcards

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4916198377elements in carbohydratescarbon, hydrogen, oxygen0
4916203722monomer in carbohydratesmonoscarite1
49162074402 monomers in carbohydratesdisacrite2
49162136433 or more monomers in carbohydratespolysacrite3
4916217059function of carbohydratesenergy plants use to build cell walls (cellulose)4
4916224775examples of carbohydratesglucose sucrose glycogen cellulose5
4916235281elements of proteinscarbon, hydrogen, oxygen, nitrogen6
4916238156monomer in proteinaminoacid7
49162409502 monomers in proteinpeptide8
49162440953 or more monomers in proteinspolypeptide9
4916253268function of proteinsspeed up chemical reactions builds immunity provides structure10
4916267129examples of proteinsenzymes anitbodies bonds muscles11
4916297090elements of nucleic acidcarbon hydrogen oxygen nitrogen phosphorous12
4916339301monomer of nucleic acidnucleotide13
4916342666polymer of nucleic acidnucleic acid14
4916359935function of nucleic acidtransmit and store genetic information (DNA contains code to make protein)15
4916374952examples of nucleic acidDNA RNA16
4916377158elements in lipidscarbon, hydrogen, oxygen17
4916408619smallest unit of a lipidfatty acid18
4916420942function of a lipidstore energy protien cell provide energy19
4916436231examples of a lipidfats and oils insulation cell membrane repels water20
491643984321

Biochemistry Flashcards

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5635827059saturated unsaturated- maxed out hydrogens on carbon bonds w/ only single bonds - has double or triple bonds in structure0
5635827966Triglyceride- made from glycerol (OH group) + fatty acid - long term energy molecule1
5635829403Phospholipids- phosphate group + fatty acid - hydrophilic on top, hydrophobic on bottom - forms cell membrane2
5635832040Protein structures- 1 - ribosomes condense amino acids to make sequence of DNA - 2 - alpha helix and beta sheets formed by hydrogen bonds and R group interactions - 3 - sulfide bonds3
5635837977Amphipathic- Charged head = hydrophylic - Noncharged bottom = hydrophobic4
5635840198Polysacchrides- polymers of sugar - Alpha = apple (bottom) - Beta = balloon (top)5
5635845390Nucleic acids- sugar + phosphate group + base pair - RNA = uracil - DNA = thymine6
5635864859Cyestine- type of amino acid that creates disulfide bonds7
5635864860Tertiary- most stable structure with most covalent bonds8
5635868110How to tell polarity- 5' ends/starts with phosphate group and carbon backbone - 3' ends with no carbon attached - new shit will add to 3' end only9
5635870738Ligase- seals gaps between okasaki fragments10
5635871265Helicase- unzips the double helix11
5635871723DNA polymerase III- replicates the leading strand12
5635872384RNA primers- cannot copy DNA without primers - inserts ribonucleotides that are eventurally p13
5635873348Topiosomerase- relieves stress of unwinding (cuts one strand)14
5635875287Alaphatic chain Alaphapatic chain- nonpolar - polar15

Biochemistry Flashcards

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4742041281Amino acids found in eukaryotes areL-amino acids0
4742043887Glycine is the onlyachiral amino acid1
4742047845Nonpolar amino acidsglycine, alanine, valine, leucine, isoleucine, methionine, proline2
4742064005Aromatic amino acidstryptophan, phenylalanine, tyrosine3
4742069498Polar side chain (non-aromatic) amino acidsSerine, threonine, asparagine, glutamine, cysteine4
4742070550Negatively charged side chain amino acidsAspartic acid and glutamic acid5
4742071787Positively charged side chain amino acidsArginine, lysine, histidine (nitrogen on side chain is protonated at physiological pH)6
4742086051pKapH at which half of the molecules of that species are deprotonated - at pH less than the pKa, a majority of the species will be protonated7
4742094374zwitterion- species with a positive and negative charge on it, cancelling out most amino acids at physiological pH - have a positive charge (amino group in acidic form) - and a negative charge (carboxyl group in basic form)8
4742105815Isoelectric pointpH at which a particular molecule carries no net charge - for AA with a neutral side group the pI is equal to the average of the two pKa values9
4742140963Peptide bond formationexample of a condensation or dehyrdation reaction b/c water is formed - C of one AA's COOH group forms a bond with N of another AA's NH3 group10
4742144850Peptides are read fromthe N-terminus to the C-terminus11
4742156352Primary and secondary structurePrimary structure: linear arrangement of amino acids Secondary structure: local structure of neighboring amino acids (B-sheets or alpha helices) - due to hydrogen bonding12
4742161524proline is often not foundin the middle of alpha helices or beta sheets - or if so it introduces a turn or kink13
4742171020Tertiary structure- folding of the protein due to hydrophobic interactions, hydrogen bonds, disulfide bonds, ionic, covalent bonds, van der waals forces14
4742175702Quaternary structure- how a polypeptide interacts with another polypeptide - not found in all proteins - immunoglobulins have 4 subunits15
4742209577Conjugated proteinsproteins with covalently attached molecules - the attached molecule is called a prosthetic group, and may be a metal ion, vitamin, lipid, carbohydrate, or nucleic acid16
4742317174Cofactors vs coenzymes- cofactors are inorganic molecules (mainly minerals) - coenzymes are organic molecules mainly the water soluble vitamins (not A,D, E, and K) - induce a conformational change in the enzyme that promotes its activity - tightly bound cofactors/coenzymes necessary for enzyme function are termed prosthetic groups17
4742351998Cooperativity and cooperative enzymes- displays a sigmoidal curve (michaelis-Menten) because of the change in activity with substrate binding Cooperative enzymes: have multiple subunits and multiple active sites - subunits may exist in a Tense (T) state: low-affinity - or a Relaxed (R) state: high affinity - one subunit changing states can affect other subunits to do the same - ex. hemoglobin18
4742369457Cooperativityrefers to the interactions b/w subunits in a multisubunit enzyme or protein. The binding of substrate to one subunit induces a change in the other subunits from the T (tense) state to the R (relaxed) state, which encourages binding of substrate to the other subunits. In the reverse direction, the unbinding of substrate from one subunit induces a change from R to T in the remaining subunits, promoting unbinding of substrate from the remaining subunits19
4742376402Enzyme activity does what with temperaturetends to double in activity for every 10 degree increase in temperature until it reaches its optimum temp20
4742478493Collagen- trihelical fiber - makes up extracellular matrix of connective tissue - important in providing strength and flexibility21
4742480644Elastin- another important part of extracellular matrix of connective tissues - primary role = stretch and recoil22
4742483868Keratins- intermediate filament proteins found in epithelial cells - contribute to the mechanical integrity of the cell - primary protein of hair and nails23
4742485018Actin- makes up microfilaments and thin filaments in myofibrils - most abundant protein in eukaryotes - have a positive side and a negative side24
4742486658Tubulin- makes up microtubules - provide structure, chromosome separation during mitosis, and intracellular transport with kinesin and dynein - has polarity like actin (negative end near nucleus)25
4742490171Myosin- primary motor protein that interacts with actin - thick filament in myofibril - crucial for sarcomere contraction26
4742492455Kinesin vs dynein- motor proteins associated with microtubules Kinesins: anterograde transport Dynein: retrograde transport27
4742499264Cell adhesion moleculesCadherins: group of glycoproteins that mediate calcium-dependent cell adhesion - two cells of the same or similar type adhered using calcium Integrins: important for binding to and communication with ECM, cellular signalling (important for clot formation) - once cell to proteins in the extracellular matrix Selectins: bind to carbohydrate molecules that project from other cell surfaces - one cell to carbohydrates, usually on the surface of other cells28
47425172333 possibilities for a when antibodies bind antigens1) neutralization of pathogen or toxin 2) opsonization - marking for destruction 3) agglutination - creating insoluble antigen-antibody complex that can be phagocytized and digested29
4742563176In electrophoresis anions move toward the ______ and cations move toward the _______cations move toward the cathode (negative charge) and anions move toward the anode (positive charge)30
4742565559SDS page Isoelectric focusingSDS page: separates protein on mass alone (SDS denatures proteins and covers them in negative charge) Isoelectric focusing: separates proteins based on their isoelectric point using a gel with the pH spectrum and an electric field, a cathode (negative charge) at the basic end of the gel will bring positively charged proteins to their pI where they will become unprotonated - opposite happens at the other end31
4742603522Bradford protein assay- Coomassie blue die is used to measure the concentration of protein - dye changes colours as it gives up protons to the protein the different colour can be measured with a spectrophotometer and compared to a known curve of protein concentration32
4742961020Enantiomersnonsuperimposable mirror images of each other - any molecule that contains a chiral carbon (4 different groups attached) and no internal planes of symmetry has an enantiomer - a compound can have only one enantiomer33
4742976241diastereomers vs epimersDiastereomers: two sugars that are in the same family that are not identical and are not mirror images of each other Epimers: a special type of diastereomers that differ in configuration at exactly one chiral center34
4742996414Alpha or beta anomersalpha anomer: -OH group of C-1 is trans to the -CH2OH Beta anomer: -OH group of C-1 is cis to the -CH2OH35
4743003056Anomeric carbonthe new chiral center formed in ring closure; it was the carbon containing the carbonyl in the straight-chain form36
4743040087Sucrose, lactose, maltoseSucrose: glucose and fructose Lactose: galactose and glucose Maltose: glucose and glucose37
4743042706Cellulose, starches, glycogenCellulose: main structural component of plant cell walls and is the main source of fiber in the human diet, made up of beta-D-glucose molecules linked by beta-1,4 glycosidic bonds Starches: main energy source for plants, glucose linked by alpha-1,6 glycosidic bonds (amylose - non branching) (amylopectin - branching) Glycogen: main energy source in animals, highly branched38
4744824759beta and alpha amylaseBeta amylase: cleaves amylose at the reducing end of the polymer to yield maltose alpha amylase: cleaves randomly along the chain to yield shorter polysaccharide chains39
4744826898glycogen phosphorylasefunctions by cleaving glucose from the nonreducing end of the glycogen branch and phosphorylating it, thereby producing glucose 1-phosphate40
4744797845Mutorationinterconversion b/w anomers of a compound41
4744801560Tautomerizationa rearrangement of bonds - ketose sugars undergo tautomerization to undergo keto-enol shifts, which forms an aldose, which then allows them to act as reducing sugars42
4744803717Anomerizationrefers to ring closure of a monosaccharide, creating an anomeric carbon (can than turn into a hemiacetal or hemiketal)43
4744891463Fully saturated fatty acidshave only single bonds - carbon is considered saturated when it is bound to four other atoms - have greater van der waals forces and are more often to be a solid at room temperature44
4744894494Unsaturated fatty acidsform one or more double bonds - double bonds introduce kinks into the fatty acid chain, which makes it difficult for them to stack and solidify - more often liquid room temp, ex. olive oil45
4744918648Glycosphingolipids, cerebrosides vs globosidesGlycosphingolipids: sphingolipids with head groups composed of sugars bound by glycosidic linkages Cerebrosides: have a single sugar Globosides: have two or more46
4744974538Terpenesodiferous steroid precursors made from isoprene, a five-carbon molecule - one terpene unit (monoterpene) contains two isoprene units47
4744975901Steroidscontain three cyclohexane rings and one cyclopentane ring - oxidation state and functional group may vary48
4744977825Prostaglandinsautocrine and paracrine hormones that regulate cAMP levels. They have powerful effects on muscle contraction, body temperature, the sleep-wake cycle, and wain49
4744986636Vitamin A (carotene)is metabolized in retinal for vision and retinoic acid for gene expression in epithelial development50
4744987569Vitamin D (cholecalciferol)metabolized to calcitriol in the kidneys and regulates calcium and phosphorus homeostasis in the intestines (increasing calcium and phosphate absorption), promoting bone formation - deficiency - rickets51
4744990686Vitamin E (tocopherols)act as biological antioxidants. Their aromatic rings destroy free radicals, preventing oxidative damage52
4744992186Vitamine K (phylloquinone and menaquinones)is important for formation of prothrombin a clotting factor. It performs posttranslational modifications on a number of proteins, creating calcium-binding sites53
4745018165Saponificationis the ester hydrolysis of triacylglycerols using a strong base - making free fatty acids - aka soup - usually use lye - soaps act as surfactant (lower surface tension at the surface of a liquid)54
4745077580More saturated fatty acids make for a ______ fluid solutionmake for a less fluid solution55
4745096279Nucleoside vs NucleotideNucleoside: composed of five-carbon sugar (pentose) bound to a nitrogen base and are formed by covalently linking the base to C-1' Nucleotides: formed when one or more phosphate groups are attached to C-5' of a nucleoside56
4745105519DNA backbonealternating sugar and phosphate - always read 5' to 3' - 3' end has free C-3' -OH group 5' end has C-5' phosphate group or -OH group57
4745109954PyrimidinesCytosine, thymine, uracil (CUT the Pye)58
4745111158PurinesAdenine, and guanine (PUre As Gold) - two rings59
4745497745Nuclesosometwo of H2A, H2B, H3A, H4A histones with 147 bp of DNA wrapped aroudn60
4745507899Heterochromatin vs EuchromatinHeterochromatin: condensed DNA, transcriptionally inactive Euchromatin: uncondensed DNA, transcriptionally active61
4745526516Helicase, DNA topoisomerase II (gyrase)Helicase: unwinds DNA Topoisomerase II: cuts DNA and relieves tension caused by twisting62
4745531318DNA polymerasesread the DNA in the 3' to 5' direction and synthase the complimentary strand in the 5' to 3' direction63
4747030925Monocistronic vs polycistronicMonocistronic: in eukaryotes, each mRNA translates into only one protein Polycistronic: in prokaryotes, each mRNA that can be translated into different proteins based on where translation begins64
4747037543Amino acids attach to which end of a tRNA molecule3' hydroxyl end65
4747040359start and stop codonsstart: AUG - methionine Stop: UAA, UAG, UGA66
4747043485The genetic code is degenerate b/cmore than one codon can specify a single amino acid ex. AAU, AAC both for Asparagine67
4747045417Missense mutationone AA substitutes for another - nonsense mutation: a premature stop codon due to a mutation68
4747076171RNA polymerase II reads in the3' to 5' direction, so that it forms RNA in the 5' to 3' direction during transcription69
4747080167Post transcriptional hnRNA processing1) splicing: get rid of introns 2) 5' methyl-7-Guanylate cap 3) 3' Polyadenylation70
4747087263Main promotor of trancriptionTATA box: thymine, adenine rich sequenced bound by TATA binding protein - ~ 25 BP upstream (-25) of transcription initiation site71
4747088585RNA pol I, II, and IIIRNA pol I: rRNA RNA pol II: mRNA & snRNA RNA pol III: tRNA (and 5S rRNA)72
4747099734Eukaryote ribosomes vs prokaryote ribosomesEukaryotes: 80S, made up 60S (5S, 5.8S, 28S) & 40S (18S) subunits Prokaryotes: 70S, made up of 50S (5S and 23 S) and 30S (16S)73
4747106992Shine-Dalgarno sequenceprokaryotes translation initiation site74
4747112250peptidyl transferaseenzyme in the large ribosomal subunit that facilitates the formation of a peptide bond, transferring the polypeptide in the E site onto the AA in the A site - uses GTP75
4747123872Operon (prokaryote gene regulation)cluster of genes transcribed as a single mRNA - very common in prokaryotes - can be - inducible (positive control):inducer removes repressor and transcription can proceed - repressible (negative control): transcription proceeds until corepressor binds repressor then bind DNA preventing transcription76
4747137471Operatorsite where repressor can bind preventing transcription of Operon77
4747177442Trp operonwhen tryptophan is present in high concentrations it acts as a corepressor - thus cell transcription of proteins used in creating tryptophan78
4747179992lac operoninduced by the presence of lactose (when glucose is low) and induces genes for lactose metabolism79
4747143161Transcription factors (eukaryote gene regulation)have two domains: activation domain and DNA-binding domain - bind DNA motif or response element and RNA pol to alter transcription80
4747151918Acetylationhistone acetylases acetylate lysine residues making them less positive and decrease their affinity to histones, therefore opening up the DNA for transcription - deacetylation = opposite81
4747155424DNA methylationsilences gene activity via chromatin remodelling - heterochromatin is much more methylated82
4747194901Sense coding strand and antisensesense coding strand is identical to the mRNA transcript - antisense is the one transcribed83
4747204962Peptide bonds are what kind of linkagesamide linkages84
4747264752Cholesterolincreases cell membrane fluidity85
4747267415Transmembrane proteins vs embedded proteinstransmembrane proteins actually traverse the membrane embedded proteins are only associated with one side of the membrane86
4747270784Gap junctions are made of6 connexin molecules which form a connexon - a hydrophilic pore that connects adjacent cells87
4747274768Desmosomesbind adjacent cells by anchoring to their cytoskeletons - interactions b/w intermediate filaments Hemidesmosomes: attach cell to underlying membranes (ECM)88
4747320345Colligative propertya physical property of solutions that is dependent on the concentration of dissolved particles, but not on the chemical identity of those dissolved particles ex. osmosis, freezing point depression, boiling point elevation, and vapour pressure depression89
4747330725Osmotic pressurea sucking force, water will move toward the compartment with the greatest osmotic pressure90
4747391552GLUT 2low-affinity glucose transporter found in hepatocytes and pancreatic cells - captures excess glucose passing through portal vein from intestine after a meal - in pancreas serves as an indicator for insulin release - if blood glucose concentrations are high, glucose will enter beta-islet cells and with glucokinase cause insulin release - km ~ 15mM91
4747399326GLUT 4in adipose and muscle - insulin causes additional GLUT 4 movement to the membrane - km ~5 mM (which is the normal glucose level in the blood) therefore when more glucose in blood, need more transporters to increase glucose intake92
4747416449Red blood cells only method of acquiring energyglycolysis b/c they lack mitochondria93
4749565337Glycolysis takes place inthe cytoplasm94
4749569312Rate limiting enzymes of 1) glycolysis: 2) fermentation: 3) glycogenesis: 4) glycogenolysis: 5) gluconeogenesis: 6) Pentose phosphate pathway:1) glycolysis: Phosphofructokinase-1 2) fermentation: lactate dehydrogenase 3) glycogenesis: glycogen synthase 4) glycogenolysis: glycogen phosphorylase 5) gluconeogenesis: fructose-1,6-bisphosphatase 6) Pentose phosphate pathway: glucose-6-phosphate deydrogenase95
4749580386Hexokinase and GlucokinaseHexokinase: present in all tissues, low km, inhibited by glucose-6-phosphate Glucokinase: present in liver and pancreatic beta-islet cells, high km, induced by insulin in hepatocytes - both use ATP and phosphorylate glucose to glucose-6-phosphate, which prevents it from leaving the cell96
4749589928Phosphofructokinase 1 (PFK-1)- rate limiting enzyme & main control point in glycolysis - converts fructose-6-phosphate to 1,6-BP and uses ATP - inhibited by: ATP, citrate, and glucagon (indirectly) - activated by: AMP, F2,6-BP PFK-2: activated by insulin, turns a small amount of F-6-P into F-2,6-BP which activated PFK-1 - inhibited by: glucagon - therefore inhibits PFK-197
4749608501Substrate level phosphorylationplacing an inorganic phosphate (Pi) onto ADP to form ATP - does not require oxygen98
4749621615Irreversible enzymes of glycolysis1) glucokinase or hexokinase 2) PFK-1 3) pyruvate kinase99
4749624598Adaption to high altitude (low pO2) involves- increase respiration - increased oxygen affinity for hemeglobin (initial) - increased rate of glycolysis - increased [2,3-BPG] in RBC (over 12-24 hour period) - normalized oxygen affinity for hemeglobin restored by the increased levels of 2,3-BPG - increased hemeglobin (over days to weeks)100
4749700431Fructose metabolismfructokinase converts to fructose-1-phosphate - aldolase B converts to glyceraldehyde and DHAP - both these are downstream from the rate limiting step of glycolysis (PFK-1), therefore high-fructose drinks supply a quick source of energy to both anaerobic and aerobic cells101
4749736043Glucogenic amino acidsall except leucine and lysine102
4749751076Insulin will _______ fructose 2,6-BP and _________ gluconeogenesis Glucagon will _______ F2,6-BP and ________ gluconeogenesisInsulin will increase F2,6-BP and inhibit gluconeogenesis Glucagon will lower F2,6-BP and stimulate gluconeogenesis103
4749755968Acetyl-CoA ______ pyruvate dehydrogenase and _______ pyruvate carboxylaseAcetyl-CoA inhibits pyruvate dehydrogenase ane stimulates pyruvate carboxylase - shift from burning pyruvate in citric acid cycle to creating new glucose molecules for rest of body - Acetyl-CoA is crucial to gluconeogenesis - the Acetyl-CoA comes from fatty acid oxidation104
4749758063Cori cycleRBC's convert glucose to lactate - lactate is delivered to the liver where it is turned into pyruvate then used for gluconeogenesis - which supplies glucose for the RBCs105
4749765032Gluconeogenic specific enzymes and what they replacepyruvate carboxylase - pyruvate kinase Phosphoenolpyruvate carboxykinase - pyruvate kinase Frucose-2,6-bisphosphatase - Phosphofructokinase 1 Glucose-6-phosphatase - glucokinase106
4749784306Two major metabolic products of the pentose phosphate pathwayNADPH and ribose-5-phosphate107
4753242861Glycolysis yields how many molecules of ATP per glucose2 ATP per glucose108
4753253009Pyruvate is _________ transported into the mitochondria after glycolysis and is oxidized and decarboxylated by pyruvate dehydrogenase complex to from _______actively transported to from Acetyl-CoA109
4753258849Pyruvate dehydrogenase complexes 5 enzymes1) Pyruvate dehydrogenase: oxidizes pyruvate and yields CO2. Mg2+ required, TPP coenzyme 2) Dihydropropyl transacetylase: lipoic acid accepts 2 carbon molecule from TPP and oxidizes it to yield an Acetyl group, Acetyl-CoA is formed 3) dihydrolipoyl dehydrogenase: FAD used to reoxidize lipoic acid, FAD reduced to FADH2, NAD+ is reduced to NADHf 4) pyruvate dehydrogenase kinase 5) Dehydrogenase phosphatase110
4753329874Citric Acid cycle rate limiting stem and enzymeD-Isocitrate to alpha-ketoglutarate - Isocitrate dehydrogenase111
4753344350Synthase vs synthetaseSynthetases: use ATP in the reaction Synthases: do not use ATP112
4753354928Please, ah, can I keep selling sex for money, officer? Mneumonic for TCA cylePyruvate, acetyl-CoA, citrate, isocitrate, alpha-ketoglutarate, succinyl CoA, Succinate, fumarate, malate, oxaloacetate113
4753385653Pyruvate dehydrogenase kinase and phosphatasePyruvate dehydrogenase kinase: phosphorylates PDH (pyruvate to Acetyl-CoA) if ATP levels are high, preventing Acetyl-CoA formation Pyruvate dehydrogenase phosphatase: reactivates PDH in response to high ADP levels - PDH also inhibited by high levels of Acetyl-CoA114
4753428445glycolysis and fermentation occurin the cytosol115
4753473361in ETC which complexes pump protons into intermembrane space? Acquire electrons from NADH Acquire electrons from FADH2 have the highest reduction potentialI, III, IV (all except II pump protons, IV is only 2 protons) Complex I acquires electrons from NADH Complex II acquires electrons from FADH2 Highest reduction pot = IV (must be last step)116
4753511791Uncouplersinhibit ATP synthesis without affecting the electron transport chain117
4753522649Pancreatic enzymes responsible for digesting fatspancreatic lipase, colipase, and cholesterol esterase - broken down into cholesterol, 2-monoacylglycerol, free fatty acids, - reform triacylglycerol and cholesteryl esters once absorbed into mucosa118
4753540468Hormone sensitive lipase- hydrolyzes triacylglycerols, yielding fatty acids and glycerol - activated by decrease in insulin levels or increase in EP or cortisol levels - active in adipose tissue119
47535485011) Chylomicrons 2) VLDL 3) IDL (VLDL remnants) 4) LDL 5) HDL1) chylomicrons: transport dietary TAG and cholesterol from intestine to tissues 2) VLDL: transport TAG from liver to tissues 3) IDL: picks up cholesterol from HDL to become LDL, picked up by the liver 4) LDL: delivers cholesterol into cells 5) HDL: picks up cholesterol in blood vessels, delivers cholesterol to liver and steroidogenic tissues, transfers apolipoproteins to other lipoproteins (considered good cholesterol)120
4753586091Alpha carboncarbon 2 of a fatty acid121
4753592884Palmitic acidprimary end product of fatty acid synthesis (16:0)122
4753604963Rate limiting step of fatty acid biosynthesisAcetyl CoA carboxylase123
4753624137Rate limiting enzyme of fatty acid oxidationCarnitine acyltransferase I: transport long-chain fatty acids (14 to 20 carbons) into the mitochondria124
4753644329Alpha-lenolenic acid lenoleic acidalpha-lenolenic acid: 18:3 all-cis-9, 12, 15, an omega-3 fatty acid Lenoleic acid: 18:2 cis,cis-9, 12, and omega-6 fatty acid (omega is the last carbon, number refers to how many carbons the first double bond is away from the omega carbon)125
4753651452excess acetyl-CoA from beta-oxidation of fatty acids is turned intoKetone bodies: transportable forms of Acetyl-CoA, produced in the liver - acetoacetate and 3-hydroxybutyrate126
4753657738Acetyl-CoA cannot be used to produceglucose via gluconeogenesis127
4753659094Ketogenesis and ketolysisKetogenesis: favored by a prolonged fast and occurs in the liver, stimulated by increasing concentrations of acetyl-CoA Ketolysis: favored during prolonged fasting, but is stimulated by low-energy state in muscle and brain tissue and does not occur in the liver128
4753666092Glucogenic Amino acidsall but leucine and lysine - can be turned into glucose via gluconeogenesis129
4753666404Ketogenic amino acidsleucine, lysine, isoleucine, phenylalanine, threonine, tryptophan, and tyrosine - can be converted to acetyl-CoA and ketone bodies130
4753692568LCAT and CETPLCAT: catalyzes the formation of cholesteryl esters for transport with HDL CETP: catalyzes the transition of IDL to LDL by transferring cholesteryl esters from HDL131
4753711872main gluconeogenesis precursorslactate, glycerol (from TAGs), alanine, and glutamine (all glucogenic amino acids, aka not leucine and lysine)132
4755579740Amino acids that are both glucogenic and ketogenicPITTT phenylalanine, Isoleucine, threonine, tyrosine, tryptophan133
4755615110Gluconeogenesis occurs mainly inthe liver and kidneys134
4755677658High energy electron carriers in cytoplasmNADH (glycolysis, fermentation, TCA, ECT), FADH2, NADPH (PPP, lipid biosynthesis, bleach formation, oxidative stress, photosynthesis), ubiquinone (ECT), cytochromes (ECT), and glutathione (oxidative stress)135
4755681917Flavoproteinssubclass of electron carriers that are derived from riboflavin (vitamin B2) - also nucleic acid derivatives (FAD - flavin adenine dinucleotide or FMN flavin mononucleotide)136
4755700510Postprandial state (well-fed state)- greater anabolism than catabolism - insulin is released with increased blood glucose levels - promotes glycogen synthesis in liver and muscle - liver converts excess glucose to fatty acids/ TAGs - promotes TAG synthesis in adipocytes - promotes protein synthesis in muscle137
4755709699Two types of cells insensitive to insulinnervous tissue and RBC's - nervous tissue uses glucose from blood (why its concentration is maintained) unless in prolonged fasting state in which switches to ketones - RBCs only use glucose anaerobically but also kidney tubules, intestinal mucosa, β-cells of pancreas - all these tissues need to take in glucose even when the concentration is low138
4755713959"Fasting state" Counterregulatory hormones (oppose insulin)glucagon, EP, NE, cortisol, and growth hormone liver: glycogenolysis, gluconeogenesis Muscle and adipose: low insulin = release of amino acids and fatty acids (sent to liver for gluconeogenesis)139
4755720442Prolonged fastingfurther elevated EP and glucagon - 24 hours - gluconeogenesis is primary energy source, glycogen stores are depleted - rapid lipolysis = excess acetyl CoA = ketone bodies - after several weeks the brain primarily uses (2/3rds) energy from ketone bodies140
4755736560Insulinpeptide hormone secreted by β-cells of the pancreatic islets of Langerhans - used for effective uptake of glucose in muscle and adipose tissue - increases glycogen synthesis in liver by increasing activity of glucokinase and glycogen synthase (decrease activities of glycogen phosphorylase and glucose-6-phosphatase) - increases amino acid uptake by muscle cells141
4755748043Insulins affect on fat metabolismInsulin increases: - glucose and TAG uptake by adipocytes - lipoprotein lipase activity - which clears VLDL and chylomicrons from the blood - TAG synthesis in liver and adipocytes from acetyl-CoA Insulin decreases: - TAG breakdown in adipose tissue - formation of ketone bodies in the liver142
4755752871Glucagonpeptide hormone secreted by α-cells of the pancreatic islets of Langerhans, primary target is hepatocytes - increased liver glycogenolysis (activates glycogen phosphorylase and inhibits glycogen synthase) - increased liver gluconeogenesis (increases pyruvate carboxylase and PEPCK activity (pyruvate to PEP) - increased liver ketogenesis and decreased lipogenesis - increases lipolysis in liver (activates hormone sensitive lipase) - glucagon is released due to low blood glucose, but also high amino acid concentration (arginine, lysine, histidine esp)143
4755763212Glucagon increasesincreases glycogenolysis, lipolysis, protein catabolism (gluconeogenesis), ureagenesis, ketogenesis, gluconeogenesis144
4755770489Cortisolglucocorticoid (steroid) released from adrenal cortex - increases lipolysis and protein catabolism, - inhibits glucose uptake in most tissues (muscle, lymph, adipose) - increases hepatic output of glucose via gluconeogenesis, particularly from amino acids145
4755776482CatecholaminesEP and NE, released from the adrenal medulla - increase activity of liver and muscle glycogen phosphorylase = more glucose output by liver - increase lipolysis via hormone-sensitive lipase146
4755786971Thyroid hormonesactivity is largely permissive (levels kept ~ constant) Thyroxine (T4) - several hour latency period and can last for several days Triiodothyronine (T3) - produces a more rapid increase in metabolic rate and shorter duration - both increase O2 consumption and heat production (aka raise basal metabolic rate)147
4755931185Ghrelinhormone secreted by the stomach in response to signals of an impending meal (sight, sound, taste, smell) - cause release of orexin148
4755932073Orexin- further increases appetite & involved in alertness & sleep-wake cycle149
4755933637Leptinsecreted by fat cells to decrease appetite by suppressing orexin production150

Biochemistry Flashcards

Terms : Hide Images
6492744409Nonpolar, Nonaromatic Side chainsglycine alanine valine leucine isoleucine methionine proline0
6492749223Aromatic side chainstryptophan phenylalanine tyrosine1
6492755579polar side chainsserine threonine glutamine asparagine cysteine2
6492762586negatively charged (acidic) side chainsaspartate glutamate3
6492769531positively charged (basic) side chainsargininge lysine histidine4
6492778076hydrophobic amino acidsalanine isoleucine leucine valine phenylalanine5
6492786520hydrophilic amino acidspositively charged histidine, arginine, and lysine negatively charged glutamate and aspartate6
6492795492AlanineAla A7
6492797433ArginineArg R8
6492803882AsparagineAsn N9
6492805992Aspartic acidAsp D10
6492809579CysteineCys C11
6492813680Glutamic acidGlu E12
6492816047GlutamineGln Q13
6492817958GlycineGly G14
6492820234HistidineHis H15
6492821931IsoleucineIle I16
6492826292LeucineLeu L17
6492827911LysineLys K18
6492829473MethionineMet M19
6492831686PhenylalaninePhe F20
6492832977ProlinePro P21
6492835067SerineSer S22
6492837058ThreonineThr T23
6492839441TryptophanTrp W24
6492841536TyrosineTyr Y25
6492842541ValineVal V26
6537646227CatalystDo not impact the thermodynamics of a biological rxn ex. Enzymes27
6537646228Enzyme classificationsOxireductase Transferase Hydrolases Lyases isomerase Ligases28
6537646229EnzymesLower the activation energy Increase the rate of rxn Don't alter the equilibrium constant Are not changed or consumed Are pH and temp. Sensitive, with optimal activity at certain temps and pH29
6537646230OxireductaseCatalyze oxidation-reduction rxn Transfer of electron from reductant to oxidant30
6537646231TransferaseCatalyse movement of functional group from one molecule to another31
6537646232HydrolasesCatalyze the breaking of compound into two molecules using the addition of water32
6537646233LyasesCatalyze the cleavage of a single molecule into two products33
6537646234IsomerasesCatalyzes the rearrangement of bonds within a molecule34
6537646235LigasesCatalyze addition or synthesis rxns generally between large similar molecules and often requires ATP35

Biochemistry Flashcards

Terms : Hide Images
6628868827the ground stateIf all the electrons in an atom are in the lowest available energy levels, the atom is said to be in...0
6628874313isotopesAtoms of one element that vary only in the number of neutrons in the nucleus (they are chemically identical)1
6628887854tracerA radioisotope that can be incorporated into a molecule and used to trace the path of a molecule in a metabolic pathway2
6628896174releasedWhen bonds are formed, is energy released or accepted?3
6628899656atoms acquire a more stable configuration by completing their outer shellWhy is energy released during bond formation?4
6628906423ionic bondA bond that results from the transfer of electrons5
6628908167covalent bondA bond that results from the sharing of electrons6
6628913741nonpolar bondThe bond when the electrons are shared equally between two identical atoms7
6628916313polar covalent bondsThe bond when the electrons are shared unequally between two atoms (whenever the bond is between two different atoms)8
6628930120polar and ionic substances (they are hydrophilic)What kinds of things dissolve in water?9
6628940570yes - oxygen is highly negative and h is highly positiveIs water polar? If so, in what way?10
6628947774a hydrogen bondA weak bond between two molecules resulting from an electrostatic attraction between a proton in one molecule and an electronegative atom in the other11
6628954181specific heatThe amount of heat a substance must absorb to increase 1 gram of the substance by 1 degree celcius12
6628958883the marine biome is very stableWhat does the high specific heat of water affect in the environment?13
6628963515water has a high heat of vaporizationWhat is important about water that relates to sweat?14
6628973719water exhibits strong cohesion tensionWhat is the phrase that means that the molecules of water tend to attract one another?15
6628979666transpirational-pull cohesion tensionThe ability of water to move up a tall tree from the roots to the leaves without the expenditure of energy (as you lose one molecule from transpiration, another takes its place)16
6628983192cohesionThe clinging of like molecules17
6628983193adhesionThe clinging of unlike molecules18
6629006378spring overturnDissolved Oxygen from the surface moves to deep water and nutrients released by decomposition moves to surface19
66290317491x10^-pH (1 units of pH has a difference of 10 times)How do you find the H+ concentration of a substance's pH in moles per liter?20
6629038460buffersSubstances that resist changes in pH21
6629042981the bicarbonate ionWhat is the most important buffer in human blood?22
6629050026carbonic acid is produced??? Pg 15What happens to the bicarbonate buffer system if there is a drop in pH?23
6629086908bicarbonate is producedWhat happens to the bicarbonate buffer system if there is a rise in pH?24
6629091066isomersOrganic compounds that have the same molecular formula but different structures25
6629096501structural isomersIsomers that differ in the arrangement of their atoms26
6629100317Cis-trans isomersIsomers that differ only in spatial arrangement around double bonds27
6629104542enantiomersMolecules that are mirror images of each other28
6629111058L-Are all the animal acids in cells L- (left handed) or D- (right handed)?29
6629188406carbon, hydrogen, and oxygenWhat are the three elements in carbohydrates?30
66291933552:1What is the ratio of hydrogen atoms to oxygen atoms in all carbohydrates?31
6629199851dehydration synthesis or condensationThe joining of two monosaccharides that releases one molecule of water32
6629203221hydrolysisThe breakdown of a compound by adding water33
6629210790glycogenA polysaccharide found in animals - "animal starch". It is stored in liver and skeletal muscle34
6629213000amylose and amylopectinWhat are two forms of starch?35
66292169901 glycerol and 3 fatty acidsWhat is the typical structure of a lipid?36
6629219469they are all hydrophobicWhy are all lipids grouped together?37
6629221255glycerolWhat is this?38
6629228796a fatty acidA hydrocarbon chain with a carboxyl group at one end39
6629233200saturated fatsFatty acids that contain only single bonds between carbon atoms40
6629237301unsaturated fatsFatty acids that have at least 1 double bond formed by the removal of hydrogen atoms in the carbon skeleton41
6629248553steroidsLipids that consist of four fused rings42
6629248554testosterone, cholesterol, etcWhat are some examples of steroids?43
6629257330to store energyWhat is the main function of lipids?44
6629258507as a major component of the cell membrane (phospholipids)Where are lipids used structurally?45
6629268069function as hormonesWhat is the function of several steroids?46
6629275895two fatty acids (hydrophobic tails) attached to the glycerol backbone and a phosphate group (hydrophilic head)What are phospholipids composed of?47
6629281909the fatty acid tailsWhat part of the phospholipid is hydrophobic?48
6629289504growth and repair, signaling, regulation, enzymatic activity, and movementWhat are the different functions of proteins in the body?49
6629294405CHNOPSWhat are the different elements in proteins?50
6629305797a carboxyl group, an amine group, the R group, and a central asymmetric carbon atomWhat do amino acids consist of?51
6629319240the R groupThis side chain differs in each amino acid52
6629322976by chemical properties: hydrophobic, hydrophilic, acidic, or basicHow are R groups categorized?53
6629328820the conformationThe unique shape of a protein54
6629335601the primary structureThe unique linear sequence of amino acids in a protein55
6629351299through peptide bondsHow are amino acids linked together?56
6629369177secondary structureThis refers to how a polypeptide coils or folds into two distinct shapes based on the hydrogen bonding within the polypeptide molecule57
6629383651a beta-pleated sheetWhat is this shape of secondary structure?58
6629389335fibrous proteinsProteins that exhibit either alpha helix or beta-pleated sheet or both59
6629395630an amino acidWhat is this?60
6629374407an alpha helixWhat is this shape of secondary structure?61
6629409942tertiary structureThe intricate 3D shape or conformation of a protein that is superimposed on its secondary structure62
6629427103Hydrogen/ionic bonding between R groups, hydrophobic interactions, Van der Waals interactions, and disulfide bonds between cysteine amino acidsWhat intramolecular factors contribute to the tertiary structure?63
6629429266quaternary structureProteins that consist of more than one polypeptide chain64
6629571438denaturationA phenomenon in which adverse conditgions alter the weak intramolecular forces, causing a protein to lose its characteristic shape as well as function65
6629582822pH, salt concentration, and temperatureWhat adverse conditions can denature a protein?66
6629716250chaperonins (chaperone proteins)Proteins that assist in folding other proteins67
6629716251prionsMisfolded proteins68
6629724069bioinformaticsThe field that studies the three-dimensional shape of proteins69
6629729301X-ray crystallographyThe study of crystals and their structure by means of X-ray diffraction - used to reveal the 3D shape of protiens70
6629742478a phosphate, a 5-carbon sugar (deoxyribose or ribose), and a nitrogen baseWhat does a nucleotide consist of?71
6629751888aminoWhat functional group is this?72
6629754528carboxylWhat functional group is this?73
6629761629hydroxylWhat functional group is this?74
6629765422phosphateWhat functional group is this?75
6629770550functional groupsThe components of organic molecules that are most often involved in chemical reactions76
6645943606asymmetric carbonA carbon atom that is attached to four different types of atoms or groups of atoms77

Biochemistry Flashcards

Terms : Hide Images
4956099259ControlBaseline of information to compare your data to0
4956099260ProcedureSteps for completing an experiment1
4956099261MaterialsSupplies needed for experiment2
4956100307VariableThe part of the experiment that is changed3
4956119211CHNOPSacronym to remember 6 elements of life4
4956119212CarbonOrganic; considered the "backbone" of life5
4956119213WaterLife-sustaining compound6
4956119214PolarHaving unequal distribution of charges7
4956120492Hydrogen BondsAttractive forces that hold together water molecules8
4956120493AtomSmallest part of an element9
4956120494ElectronsNegatively charged particles10
4956121713CohesionWhen water sticks to water11
4956121714AdhesionWhen water sticks to something else12
4956121715Universal SolventThe ability to dissolve any substance (ex. water)13
4956122866BiomoleculesThe molecules of life: carbs, lipids, proteins, nucleic acids14
4956122867Proteintype of biomolecule, provide structure to the body, made of amino acids15
4956122868Lipidtype of biomolecule, provide long-term energy, made of fatty acids16
4956122869Carbohydratestype of biomolecule, provide short-term energy, sugar, made of monosaccharides17
4956124764Nucleic Acidstype of biomolecule, store genetic information, DNA/RNA, made of nucleotides18
4956125801DNAexample of Nucleic Acid, has bases A, T, C, G19
4956125802RNAexample of Nucleic Acid, has bases A, U, C, G20
4956128771Enzymetype of protein that speeds up chemical reactions21
4956128772Amino Acidsmonomer (building block) of protein22
4956128773Polypeptidepolymer of protein23
4956130426Hydrophilicloves water24
4956130427Hydrophobicafraid of water25
4956130428FatsExample of lipid26
4956130429InsulationFunction of lipids27
4956131737ProtectionFunction of Lipids28
4956131738Quick energyFunction of carbs29
4956132986Long-term energyFunction of lipids30
4956134025Store genetic informationFunction of nucleic acids31
4956134026StructureFunction of proteins32
4956135691GlucoseMain type of sugar33
4956135692A-S-EEnzymes end in these 3 letters34
4956135693O-S-ESugars end in these 3 letters35
4956135694O-LAlcohols end in these 3 letters36
4956135695SaccharideLatin word for sugar37
4956137149Monosaccharidesingle sugar (monomer of carbs)38
4956137150Polysaccharidepolymer of carbs39
4956137151Starchcomplex carb, found in bread40
4956138342Nucleotidesmonomers of nucleic acids41
4956139649A, T, C, Gbases of DNA42

Biochemistry Flashcards

Terms : Hide Images
5058219750AtomsTiny units that make up living and nonliving things0
5058219751NucleusThe center core of the atom1
5058219752NeutronNo electrical charge2
5058219753ElectronNegatively charged particles3
5058219754ProtonPositively charged particles4
5058219755ElementA substance made up entirely of one kind of atom5
5058219756CompoundFormed when 2 or more elements chemically combine6
5058219757Chemical BondingThe process by which 2 elements combine7
5058219758MoleculeA small particle of an element or compound capable of independent motion8
5058219759Chemical FormulaRepresents the chemical makeup of a compound. Ex. Carbon Dioxide- CO29
5058219760Structural FormulaThe formula that shows the kinds, numbers, and arrangement or atoms. Ex. Carbon Dioxide- O=C=O10
5058219761EquationUsed to describe chemical reactions11
5058219762ReactantThe substances that start the reaction. On the left side of the equation12
5058219763ProductSubstances formed by the reaction. Placed on the right side of the equation13
5058219764Inorganic CompoundCompounds that do not contain both Carbon and Hydrogen14
5058219765Organic CompoundCompounds that contain Carbon and Hydrogen15
5058219766CarbohydratesMain source of energy for cell activities. Formed by carbon, hydrogen, and oxygen. Ex. Starch and Sugars16
5058219767MonosaccharideSimple sugars. Building blocks of carbohydrates. Ex. Glucose17
5058219768DissaccharideDouble sugar. Ex. Maltose.18
5058219769GlucoseCommon monosaccharide. Formed during photosynthesis. C6H12O619
5058219770MaltoseCommon dissaccharide. Formed when 2 glucose molecules chemically combine20
5058219771PolysaccharideLong chains of monosaccharides bonded together. Ex. Starch and cellulose21
5058219772LipidsFats and oils. Contain carbon, hydrogen, and oxygen. Form part of the structure in a cell membrane. Source of stored energy.22
5058219773FatsLipids that are solid at room temperature.23
5058219774OilsLipids that are liquid at room temperature24
5058219775Fatty acids and GlycerolBuilding blocks of lipids25
5058219776ProteinForm important cell products such as enzymes, many hormones, antibodies, and hemoglobin. Made up of carbon, hydrogen, oxygen, and nitrogen. Composed of amino acids. Made of long polypeptide chains26
5058219777Amino acidBuilding blocks of proteins. 20 _______ in living things.27
5058219778Dipetide2 amino acids bonded together28
5058219779PolypeptideMany amino acids bonded together29
5058219780EnzymeLarge complex protein molecules that control the rate of chemical reactions. The organic catalysts in cellular chemical reactions. Each chemical reaction that occurs in a living thing is controlled by this.30
5058219781CatalystSomething that speeds up or slows down chemical reactions.31
5058219782Nucleic AcidLarge molecules made up of carbon, oxygen, nitrogen and phosphorus.32
5058219783NucleotideSimplest unit of nucleic acids. Composed of a sugar molecule, a nitrogen base, and a phosphate group.33
5058219784DNAMakes up genes and is involved in heredity34
5058219785RNAInvolved in the synthesis of proteins35
5058219786PH scaleMeasures whether a solution is acid, basic, or neutral. Runs from 0-14. 7 is neutral. Lower the number stronger the acid. Higher than 7 is base36

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