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Biochemistry Flashcards

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6726197145What is an atom made of?Protons, neutrons and electrons0
6726197146What is the charge of an atom?Neutral because the number of protons and electrons are equal1
6726197147What is the charge of a proton?+2
6726197148What is the charge of an electron?-3
6726197149What is ground state?When all the electrons in the atom have the worst available energy levels4
6726197150What is it called when the electrons in the atom are at a high level of energy?Excited state5
6726197151What are isotopes?Atoms of one element that vary only in the number of neutrons in the nuclues6
6726197152Where are the neutrons and protons located?The nucleus7
6726197153Where are the electrons located?The electron clouds8
6726197154What is a half life?The time it takes from a radioactive isotope to decay in half9
6726197155What are radioactive isotopes called?Radioisotopes10
6726197156What can radioactive iodine be used for?Diagnose and treat thyroid diseases11
6726197157What is a tracer?A radioactive isotope that can be incorporated into the biological pathways to track the movement of certain elements12
6726197158What is released when a bond is formed?Energy13
6726197159What must be applied to break a bond?Energy14
6726197160What is an ionic bond?Electrons are transformed15
6726197161What is the atom that loses an electron called?Cation16
6726197162What is the ion that gains an electron called?Anion17
6726197163What is a covalent bond?Electrons are shared18
6726769531What is the structure created by a covalent bond called?A molecule19
6726769532What is the bond called if the electrons are shared equally?Nonpolar20
6726769533Where is this type of bond found?Diatomic molecules21
6726769534What is the bond called if the electron are not shared equally?Polar covalent bond22
6726769535What does hydrophilic mean?Will dissolve in water (polar) miscible23
6726769536What is water known as?The universal solvent24
6726769537What does hydrophobic mean?Does not dissolve in water (nonpolar) not miscible25
6726769538What is the plasma membrane made of?Phospholipid bilayer26
6726769539What can cross the plasma membrane?Nonpolar molecules27
6726769540Is water polar or nonpolar?Polar28
6726769541What has the negative charge in water?Oxygen29
6726769542What has the positive charge in water?Hydrogen30
6726769543What bond holds water together?Hydrogen bond31
6726769544Is a hydrogen bond strong or weak?Weak32
6726769545What does the high specific heat capacity of water do for the environment?It prevents large bodies of changing temperature drastically so the marine biome can survive33
6726769546What does the high heat of vaporization water do for humans?Evaporating water requires absorption of heat, so evaporation of sweat cools the body surface34
6726769547AdhesionThe attraction between water and another substance35
6726769548CohesionThe attraction between water molecules36
6726769549What does adhesion and cohesion allow?Transpirational-pull cohesion tension, capillary action and surface tension37
6726769550Is water less or more dense as a solid?Less dense which allows ice to float and is why marine life survives during the winter38
6726769551What is the spring overturn?When the ice melts the water becomes denser and sinks to the bottom causing the nutrients to be filtered to the top of the water39
6726769552What is pH?A measure of the acidity and alkalinity of a solution40
6726769553What is a ph of 7 considered?Neutral41
6726769554What is pH lower than 7 considered?Acidic42
6726769555What is a pH higher than 7 considered?Basic43
6726769556What is the difference between one pH level?Times 1044
6726769557What is the pH of human blood?7.445
6726769558What is the concentration of hydrogen at acidic?Higher46
6726769559What is the concentration. If hydrogen at basic?Lower47
6726769560What are buffers?Substances that prevent pH change48
6726769561What is the most important buffer in the human body?Bicarbonate ion49
6726769562What are isomers?Organic compounds that have the same molecular formula but different structure50
6726769563What are structural isomers?Differ in the arrangement of their atoms51
6726769564What are CIs-trans isomers?Differ only in the spatial arrangement around double bonds (less flexible than single bonds)52
6726769565What are enantiomers?Are molecules that are mirror images of each other (L and D versions)53
6726769566What are all living organisms made of?Organic compounds (carbon)54
6726769567What are the four types of organic molecules?Carbonhydrates, lipids, proteins, and nucleus acids55
6726769568What are carbohydrates used for in the body?Fuel and building materials56
6726769569What are monosaccharides?Glucose, galactose, and fructose57
6726769570What are disaccharides?Two monosaccharides58
6726769571How are disaccharides made?The removal of water called dehydration synthesis of condensation?59
6726769572Glucose + glucose =Maltose60
6726769573Glucose + galactose=Lactose61
6726769574Glucose +fructose=Sucrose62
6726769575What is hydrolysis?The breakdown of a compound by adding water63
6726769576What are polysaccharides?Macromolecules of monosaccharides64
6726769577What polysaccharides are used in plants?Cellulose (makes up the cell walls) Starch (storage amylose and amylopectin)65
6726769578What polysaccharides are used in animals?Chitin (make up the exoskeleton of animals) Glycogen (strode in human liver)66
6726769579What are lipids?Fats, oil, waxes and steroids67
6726769580Are lipids hydrophilic or hydrophobic?Hydrophobic68
6726769581What are lipids made of?3 fatty acids and a glycerol69
6726769582What is a fatty acid?A hydrocarbon chain with a carbonyl group70
6726769583What do saturated fatty acids have?Single bonds71
6726769584What do unsaturated fatty acids have?At least one double bond72
6726769585Whoa are steroid's structure?They consist of four fused rings73
6726769586How are lipids used in energy storage?Lipids release energy when burned74
6726769587How are lipids used structurally?Phospholipids make up the cell membrane75
6726769588How are lipids used in the endocrine system?Steroids are hormones76
6726769589What is the structure of a phospholipid?2 hydrophobic tails facing the inside and a hydrophilic head on the outside77
6726769590What are the functions of proteins?Growth and repair Signaling from one cell to another Regulation: hormone Enzymatic activity Movement (muscle contractions)78
6726769591What are proteins made of?Polymers or polypeptides of amino acids?79
6726769592What bond makes up proteins?Polypeptide bond80
6726769593What makes up an amino acid?A carbonyl group, an amine group and an R group81
6726769594What determines the function of the protein?The shape or conformation82
6726769595What is the primary structure of proteins?Linear sequence of amino acids83
6726769596What is the secondary structure of proteins?Hydrogen bonds within polypeptide causes the shape to start to form (alpha helix of beta pleated sheet)84
6726769597What are secondary proteins called?Fibrous proteins85
6726769598What secondary protein make sup human hair?Keratin86
6726769599What is the quaternary structure?Multiple polypeptide chains bonding87
6726769600What is the tertiary structure?3-D shape88
6726769601What does the tertiary structure determine?Specificity89
6727117082What is it called when a change in the environment causes the protein to lose its shape?Denaturing90
6727117083What helps fold proteins?Chaperone proteins or chaperonins91
6727117084What are prions?Proteins that cause disease caused by the misfolding of other proteins92
6727117085What three techniques reveal the 3 D structure of proteins?X-ray crystallography, unceasing magnetic Resonance and bioinformatics93
6727117086What are the two types of nuclear acids?RNA (ribonucleic acids) and DNA (deoxyribonucleic acids)94
6727117087What are nuclear acids made of?Nucleotides95
6727117088What are nucleotides made of?Phosphate, 5-carbon sugar and a nitrogen base96
6727117089What are the bases?Adenine and thymine (DNA) or uracil (RNA) Cytosine and guanine97
6727117090What are functional groups?The components of organic molecules that is involved of the chemical reaction98
6727117091What is the compound hydroxyl makes?Alcohol99
6727117092What is the first law of thermodynamics?Energy can not be created or destroyed just transferred (law of conservation of energy)100
6727117093What is the second law of thermodynamics?During energy conversions, entropy (the disorder of the universe) is increased101
6727117094What is Gibb's free energy?Energy available to do work in the cell102
6727117095What is it called when a reaction releases energy?Exergonic103
6727117096What is it called when a reaction absorbs energy?Endergonic104
6727117097Exergonic reactions power Endergonic reactions so they are considered?Coupled105
6727117098What is Metabolism?The sum of all chemical reactions that take place in a cell106
6727117099What are reactions that break down molecules called?Catabolism107
6727117100What are reactions that build up molecules called?Anabolism108
6727117101Metabolic reactions take place in?Pathways109
6727117102What do enzymes do?They are catalytic proteins that spend up a reaction by lowering the activation energy110
6727117103What is the transition state?The reactive (unstable) condition of the substance after sufficient energy has been absorbed111
6727117104What are enzymes?Globular proteins and exhibit the tertiary structure112
6727117105What does an enzyme bind to?A substrate113
6727117106What is an induced-fit?A substrate binds to an enzymes active site and the enzyme alters it shape to better fit the substrate114
6727117107What is an enzyme bound to a substrate called?An enzyme-substrate complex115
6727117108What are coenzymes?Enzymes that help enzymes (vitamins)116
6727117109What are cofactors?Inorganic molecules that help enzymes117
6727117110What is competitive inhibition?Regulate enzymes by competing inhibitors bindi to the active site of the enzyme118
6727117111What is no competitive inhibition?Noncompetitive inhibitors of allosteric regulators bind to the allosteric site and it alters the shape of the enzyme preventing it to bind to substrates119
6727117112What is feedback inhibition in noncompetitive inhibition?The end product if the pathway is a the Eric inhibitor for an enzyme that catalysts an early step in the pathway120
6727117113What is cooperativity?Allosteric activation that binds to an enzyme and keeps it activcated121
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Biochemistry I Exam II Flashcards

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12111398237ProteinsWhat is the most abundant biomolecule in the body?0
12111416769GlycineWhat is the only amino acid that lacks a chiral center?1
12111422268C-terminalWhat part of the amino acid contains a carboxylic acid?2
12111427364N-terminalWhat part of the amino acid contains an amine group?3
12111435971L-chiralWhat type of chirality has a CRN clockwise arrangement?4
12111451559D-chiralWhat type of chirality has a CRN counterclockwise arrangement?5
12111458271RacemicIf the chiral center is a 50-50 mixture of L and D it is referred to as what?6
12111468811L-chiralAlanine has what chirality?7
12111479144AlanineWhich amino acid functions to make new glucose? (Gluconeogenesis)8
12111530151AliphaticWhat is the term for an R group that contains a hydrocarbon?9
12111564989LeucineWhich amino acid is metabolized into the cholesterol precursor HMG CoA?10
12111583033ValineWhich amino acid is responsible for the improper folding of red blood cells?11
12111588839HemoglobinValine replaces glutamate and causes improper folding in what structure of a red blood cell?12
12111601438Maple Syrup Urine DiseaseWhat disorder occurs when infants are unable to metabolize branched chain amino acids?13
12111620655Sickle cell anemiaWhat genetic mutation occurred in order to prevent malaria, but causes improper folding of RBC's?14
12111640071MethionineWhich amino acid contains a sulfur and is a precursor for a very import myelinating molecule?15
12111652511ProlineWhich amino acid disrupts a-helix and B-pleated sheet formations in secondary structure folding of proteins?16
12111676928PhenylalanineWhich amino acid is a precursor for tyrosine?17
12111683899Phenylketonuria (PKU)What disorder is a result of decreased metabolism for the amino acid phenylalanine?18
12111698380TryptophanWhich amino acid is a precursor for serotonin, melatonin, and niacin?19
12111705402TyrosineWhich amino acid is a precursor for thyroxine and is very important to the beginning pathways of cell signaling? I.e- RTK pathways20
12111725109Very low proteinWhat should someone with PKU ingest in their diet?21
12111731353Cystic FibrosisWhat is the most common genetic disorder?22
12111749106Serine and threonineWhich amino acids main function is to H bond to other molecules in protein regulation pathways?23
12111766687CysteineWhich amino acid contains a thiol (SH group) that acts as an antioxidant?24
12111780794GlutamineWhich amino acid is the main nitrogen carrier and is primarily synthesized in the brain?25
12111795037HistimineWhat molecule is important for its buffering capacity in hemoglobin?26
12111835933HydroxylysineWhich amino acid derivative is found in collagen?27
12111841904Isoelectric pointWhen are amino acids least soluble?28
12111852917pK1Which pK is a measure of the dissociation of the carboxylic acid group (C-terminal) on an AA?29
12111865757pK2Which pK is referring to the amine group of an AA?30
12111871070pKRWhich pK is referring to the dissociation of protons from the R group on an amino acid?31
12111886957ZwitterionWhat is the term that describes the net neutrality of an amino acid?32
12111903668Isoelectric point (pI)What is the point where an AA or protein is a zwitterion (neutral)?33
12111911098net positiveWhat is the charge when pH34
12111919626Net negativeWhat is the charge when pH>pI?35
12112091397Dehydration reactionsWhat type of reaction is involved in the synthesis of ALL macronutrients?36
12112119951GlutathioneWhat is the smallest peptide?37
12112124426pKRWhich pK group is the most important group for buffers?38
12112134821Conjugated proteinsWhat is a protein that has chemical constituents? i.e- glycoproteins and metalloproteins39
12112155246ConformationWhat is the spatial arrangement of atoms within a protein?40
12112159237Native conformationWhat is it called when a protein is in its most stable, functional conformation?41
12112198692HydrophobicWhat type of amino acids are buried in the middle of a structure, away from water?42
12112208272PrimaryWhat level of protein structure is just the order in which amino acids are aligned?43
12112222295SecondaryWhat level of structure contains a-helix, B-sheets, and B-turns?44
12112244829Beta turnsWhat reverses the direction of polypeptides from parallel to anti-parallel?45
12112280593QuaternaryWhat level of structure consists of two or more polypeptide strands that fold over and bond by non-covalent interactions? i.e- hemoglobin46
12112295575Primary and tertiaryWhich levels of structure use covalent (true) bonds?47
12112303110FourHow many different polypeptide strands make up hemoglobin?48
12112310608FibrousWhat type of protein contains a single secondary structure, and functions to provide support?49
12112319463GlobularWhat type of proteins have several secondary structures and make up enzymes?50
12112336039GlycineWhat AA does collagen have the most of?51
12112344264Triple helixWhat type of structure is collagen?52
12112348972ScurvyWhat disorder occurs from a lack of vitamin C?53
12112355337Vitamin CWhat is required for hydroxylation of proline and lysine in collagen synthesis?54
12112374068Posttranslational modificationWhat is the term that describes the addition of a functional group after the protein is synthesized?55
12112388002Proline hydroxylase and lysyl hydroxylaseWhat requires vitamin C to add a hydroxyl group to proline and lysine?56
12112420064Lysyl oxidaseWhat compound deaminates lysine and forms a reactive aldehyde?57
12112427164Copper (Cu)What is lysyl oxidase dependent upon?58
12112436447Matrix metalloproteins (MMP's)What degrades collagen?59
12112452166MotifWhat pattern of folding is not inherently stable?60
12112455830DomainWhat is the part of a polypeptide chain that is independently stable?61
12112501064Entropy (S)As a protein is folded what decreases?62
12112529158ChaperonesWhat are the molecules that assist in the folding of proteins?63
12112563003Degraded or accumulatedWhat happens to a protein if it misfolds?64
12112579913ProteostasisWhat process controls protein synthesis, folding, refolding, and degradation of proteins?65
12112647689Globular proteinsWhat type of proteins are easily denatured?66
12112657438intrinsically unstructured proteins (IUPs)What is a protein that has no specific structure on at least part of it?67
12112666903Signaling pathwaysWhat are IUP's important for?68
12112678124Metamorphic proteinsWhat are proteins that are able to form multiple structures that all have different functions?69
12112729253LigandWhat are molecules that are reversibly bound by a protein?70
12112740343Induced fitWhat is the structural adaptation of a protein in which a conformational change occurs for the the binding of a ligand?71
12112759677OneHow many oxygens can myoglobin carry?72
12112763504FourHow many oxygens can hemoglobin carry?73
12112771735OneIf a protein has one polypeptide strand (heme), how many oxygens can it carry?74
12112789336RelaxedIf a hemoglobin is acting as oxyhemoglobin and has a high affinity for binding oxygen, it is in which state?75
12112835450TenseIf a hemoglobin is acting as deoxyhemoglobin and has a low affinity for binding oxygen, it is in what state?76
12112849693Cooperative bindingWhat term describes the ability of oxygen to bind as more oxygen binds in a hemoglobin?77
12112864565High and easyWhat is the affinity for oxygen to bind to a hemoglobin if the hemoglobin already has three O2 bound? How difficult will it be for the last oxygen to bind?78
12112953203AllostericIf interactions of compounds affect the ability of heme groups to bind oxygen, it is said to be what?79
12112983534Deoxyhemoglobin (tense)A decrease in pH shifts the hemoglobin towards what state?80
12112988049Oxyhemoglobin (relaxed)An increase in pH shifts the hemoglobin towards what state?81
12113032371Low affinityIs affinity for oxygen high or low in peripheral tissues?82
12113050641Carbon monoxide (CO)What has a 250 times higher affinity to bind to iron in hemes than oxygen?83
12113073308Doesn't allow for release of O2 in tissuesWhat effect does CO have on the oxygen in hemoglobin?84
12113084056Hemolytic and obstructiveWhat are the types of jaundice?85
12113105859HemolyticWha type of jaundice has high levels of unconjugated bilirubin?86
12113115769ObstructiveWhat type of jaundice is able to excreted in the kidneys and has high levels of conjugated bilirubin?87
12113148859IgGWhat class of immunoglobulins is most common?88
12113152095IgAWhat class of immunoglobulins is found in secretions (tears, saliva, breastmilk)?89
12113157096IgEWhat immunoglobulin is the main antibody produced in response to food allergies?90
12113167194IgMWhat immunoglobulin is the first antibody produced during an immune response?91
12113697907Speed up reactionsWhat is the primary function of an enzyme?92
12113702873NoAre enzymes consumed in a reaction?93
12113706239CofactorWhat is the inorganic component of an enzyme?94
12113709064CoenzymeWhat is the organic component of an enzyme?95
12113723612VitaminsWhat are often used as coenzymes ?96
12113739639ApoenzymeWhat is the protein part of an enzyme?97
12113758803HoloenzymeWhat is the complete, active enzyme called? (The "whole" enzyme)98
12113773766ZymogenWhat is the inactive enzyme precursor called?99
12113782312End in "-ogen" or begin with "pro"How do you distinguish an inactive enzyme from an active one?100
12113800619OxidoreductaseWhat class of enzymes involves the addition or removal of H+? REQUIRES NAD+ or FAD101
12113816026TransferaseWhat class of enzymes involves the transfer of a functional group? Will often involve ATP, ending with a phosphate being bound to the product102
12113829485TwoHow many reactants and products will be involved in transferase?103
12113840816IsomeraseWhat class of enzymes rearrange functional groups on one molecule? Only involves one reactant and one product104
12113853237HydrolaseWhat class of enzymes causes hydrolysis to break bonds? Water is a reactant.105
12113859983LyaseWhat class of enzymes cleaves C-C, C-S, or C-N bonds ?106
12113868736LigaseWhat class of enzymes is the only class that involves the formation of bonds, and typically uses ATP, but results in a free phosphate group?107
12113988606Active siteWhat is the part of an enzyme that contains a binding site and a catalytic site?108
12114023448induced fitWhich active site model is the most common and allows for the enzyme to "mold" into a form where the substrate can bind?109
12114045305Binding energyWhat is the energy released through the formation of weak bonds in the active site?110
12114078828KMWhat is equal to one half of V Max?111
12156291279Vo is dependent on [S]What happens if [S]<112
12156302631Vo is dependent on both [E] and [S]What happens if [S]>Km?113
12156316490Vo is dependent on [E], enzyme is saturated with SWhat happens if [S]>>Km114
121563463401/VmaxWhat is the y-intercept of a line weaver burke plot?115
12156355463-1/KmWhat does the x-intercept of a Lineweaver-Burk plot represent?116
12156363077Km/VmaxWhat is the slope of a lineweaver burke plot?117
12156387957The number will be biggerWhat will happen if the line is closer to the origin of a lineweaver burke plot?118
12156404528[E]What does velocity of enzyme and substrate reactions depend on?119
12156415599Decrease enzyme activityWhat happens if there is a deficiency in vitamins or minerals?120
12156426734Increase in rateWhat happens to the enzyme if there is an increase in temperature?121
12156445214pH 1.5What is the optimum pH of pepsin?122
12156449814pH 6.2What is the optimum pH of sucrase?123
12156452882pH 6Wha tis the optimum pH of polyphenol oxidase?124
12156463340Denaturation of the enzymeWhat will extreme temperatures and pH do to the enzyme?125
12156475563Covalent bondsWhat type of bond is in irreversible inhibitor reactions?126
12156480612Noncovalent bondsWhat kind of bond is in reversible inhibitor reactions?127
12156494344Active siteWhere will a competitive inhibitor bind to?128
12156505301Increased Km and no change in VmaxWhat effect does a competitive inhibitor have on Km and Vmax?129
12156530563Only binds the complexWhat will an uncompetitive inhibitor bind to?130
12156541814Decreases Km and decreases VmaxWhat effect does the uncompetitive inhibitor have on the Km and Vmax?131
12156569456Active site or complexWhat will the noncompetitive inhibitor bind to?132
12156580157Decreases Vmax and doesn't change KmWhat is the effect of the noncompetitive inhibitor on Km and Vmax?133
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