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Biochemistry Complete

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191919609ionic bondbond resulting from a transfer of electrons (electrons being ripped off)
191919610covalent bondbond resulting from the sharing of electrons
191919611nonpolarelectrons shared equally
191919612polar covalent bondbond resulting from electrons shared unequally
191919613buffersubstance that resists changes in pH
191919614bicarbonate ionmost important buffer in human blood
191919615isomerorganic compounds with the same molecular formula but different structure
191919616monosaccharideC6H12O6 simple sugar; glucose, galactose, and fructose
191919617disaccharidetwo monosaccharides joined together; C12H22O1; maltose, lactose, and sucrose
191919618dehydration synthesiscondensation; joining compounds together with water released
191919619hydrolysisbreakdown of a compound by adding water
191919620polysaccharidepolymers of carbohydrates ("many" sugars)
191919621cellulosestructural polysaccharide that makes up plant cell walls
191919622starchstorage polysaccharide found in plants
191919623amylosesimplest storage polysaccharide form of starch
191919624amylopectinmore complex storage polysaccharide form of starch
191919625chitinstructural polysaccharide found in animals; makes up the exoskeleton in arthropods
191919626glycogenstorage polysaccharide animal starch that in humans is stored in the liver and the skeletal muscle
191919627glycerolalcohol portion of a lipid
191919628fatty acidhydrocarbon chain with a carboxyl group at one end; attaches to glycerol
191919629saturated fatfat without double bonds
191919630unsaturated fatfat with double bonds
191919631steroidlipid with a four fused ring structure; cholesterol and testosterone
191919632peptide bondbond creating amino acid chains or polymers (bond between amino acids)
191919633conformationprotein's unique shape that determines its function
191919634primary structurelinear sequence of amino acids; peptide bonds
191919635secondary structureprotein formed with hydrogen bonds
191919636tertiary structure3D conformation formed; determines specificity, due to hydrogen bonds, disulfide bridges, hydrophobic interactions and ionic bonds
191919637quaternary structureprotein with more than one polypeptide chain
191919638alpha helixsecondary structure form of a protein; human hair (keratin)
191919639beta pleated sheetsecondary structure form of a protein; spider webs and silk
191919640heme groupone of four polypeptide chains in the quaternary structure of hemoglobin
191919641protein folding problemhow proteins form their unique shapes
191919642functional groupcomponents of organic molecules most often involved in chemical reactions
191919643metabolismsum of all chemical reactions that take place in cell
191919644enzymecatalytic protein that lowers a reaction's energy of activation
191919645induced fit modelenzyme model where the substrate induces the enzyme to alter its shape slightly so it fits better
191919646cofactorinorganic enzyme assist
191919647coenzymeorganic enzyme assist (vitamins)
191919648competitive inhibitioncompounds that look like the normal substrate compete for the same active site on the enzyme
191919649noncompetitive inhibitionmore than one active site and the substrates do not look like each other
191919650allosteric inhibitiontwo active sites, one for a substrate and one for an inhibitor
191919651feedback inhibitionmetabolic pathway is switched off by the end product; allosteric inhibition
191919652cooperativitysubstrate stimulating an enzyme with quaternary structure to be more effective
191919653cohesionlike molecules sticking together
191919654alkalinesynonym for basic
191919655saltcompound that releases ion other than H+ or OH- when dissolved in water
191919656chemical equilibriumwhen the reaction rate is about the same in either direction
191919657polymerlong molecule consisting of many similar or identical monomers linked together
191919658monomerbuilding block for polymers; only made by producers
191919659adhesionattraction between different kinds of molecules
191919660surface tensionmeasure of how difficult it is to stretch or break the surface of a liquid
191919661van der Waals interactionstertiary structure; weak attractions between molecules or parts of molecules that result from localized charge fluctuations
191919662evaporative coolingproperty of a liquid where the surface becomes cooler during evaporation due to the loss of molecules
191919663hydration shellsphere of water molecules around each dissolved ion
191919664disulfide bridgetertiary structure; strong covalent bond formed when one sulfur of one cysteine monomer bonds to the sulfur of another
191919665hydrophobic interactiontertiary structure; weak chemical bond formed when molecules that do not mix with water change to exclude the water
191919666hydrocarbonorganic molecule consisting of only hydrogen and carbon
191919667macromoleculegiant molecule formed by the joining of smaller molecules
191919668glycosodic linkagecovalent bond formed between two monosaccharides by a dehydration synthesis reaction
191919669triosethree carbon sugar
191919670pentosefive carbon sugar
191919671hexosesix carbon sugar
191919672hydroxylhydrogen bonded to oxygen bonded to an organic molecule's carbon skeleton; alcohol; polar
191919673carboxyloxygen double bonded to a carbon atom that is bonded to a hydroxyl group
191919674aminenitrogen bonded to two hydrogens and to the carbon skeleton
191919675phosphatephosphorous bonded to four oxygens, two have negative charges, one is bonded to the carbon skeleton; phospholipid
191919676isotopeatoms with same number of protons but different number of neutrons
191919677hydrogen bondweak bond between hydrogen and a highly electronegative atom like nitrogen or oxygen
191919678acidmore H+ than OH- ions, pH below 7
191919679basemore OH- than H+ ions, pH above 7
191919680pHmeasure of H+ ions in a solution
191919681triglycerideglycerol plus 3 fatty acids
191919682phospholipidhas a hydrophilic head and hydrophobic tail, major component of cell membrane
191919683LDLlow density lipoprotein, "bad cholesterol"
191919684HDLhigh density lipoprotein, "good cholesterol"
191919685amino acidcontain carboxyl group (COOH) and amino group (NH2) and side chain R.... make up proteins
191919686chaperonina protein that assists in the proper folding of a polypeptide into a protein

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