[scholar.biology.medicine] biochemistry (3rd ed 2004) d. voet & j. voet chapter 08 (threedimensional structures of proteins)外语英文电子书

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1、7884d_c08.qxd1/2/038:16AMPage219mac62mac62:1st_TC:Chapter8Three-DimensionalStructuresofProteins1SecondaryStructurehaverathersimilarcharacteristics,akindofhomogeneousA.ThePeptideGroup“average”oftheirrandomlydanglingsidechains.How-B.HelicalStructuresever,the

2、three-dimensionalstructureofanative(physio-C.BetaStructureslogicallyfolded)proteinisspecifiedbyitsprimarystruc-D.NonrepetitiveStructuresture,sothatithasauniquesetofcharacteristics.2FibrousProteinsInthischapter,weshalldiscussthestructuralfeaturesA.Keratin—

3、AHelixofHelicesofproteins,theforcesthatholdthemtogether,andtheirB.Collagen—ATripleHelicalCablehierarchicalorganizationtoformcomplexstructures.This3GlobularProteinswillformthebasisforunderstandingthestructure–func-A.InterpretationofProteinX-RayandNMRtionrel

4、ationshipsnecessarytocomprehendthebiochemi-Structurescalrolesofproteins.DetailedconsiderationofthedynamicB.TertiaryStructurebehaviorofproteinsandhowtheyfoldtotheirnativeC.StructuralBioinformaticsstructuresisdeferreduntilChapter9.4ProteinStabilityA.Electros

5、taticForcesB.HydrogenBondingForces1SECONDARYSTRUCTUREC.HydrophobicForcesD.DisulfideBondsApolymer’ssecondarystructure(2structure)isdefinedE.ProteinDenaturationasthelocalconformationofitsbackbone.Forproteins,F.ExplainingtheStabilityofThemostableProteinsthis

6、hascometomeanthespecificationofregularpolypep-5QuaternaryStructuretidebackbonefoldingpatterns:helices,pleatedsheets,andA.SubunitInteractionsturns.However,beforewebeginourdiscussionoftheseB.SymmetryinProteinsbasicstructuralmotifs,letusconsiderthegeometrical

7、C.DeterminationofSubunitCompositionpropertiesofthepeptidegroupbecauseitsunderstandingAppendix:ViewingStereoPicturesisprerequisitetothatofanystructurecontainingit.A.ThePeptideGroupThepropertiesofaproteinarelargelydeterminedbyitsInthe1930sand1940s,LinusPaulin

8、gandRobertCoreythree-dimensionalstructure.OnemightnaivelysupposedeterminedtheX-raystructuresofseveralaminoacidsandthatsinceproteinsareallcomposedofthesame20typesdipeptidesinanefforttoelucidatethestruct