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1、NuclearMagneticSecondaryarticleResonanceSpectroscopyofArticleContents.IntroductionProteins.NMRStructureDeterminationofProteins.NewExperimentalApproachesforHigh-molecularMassSystemsKurtWu¨thrich,SwissFederalInstituteofTechnology(ETH),Zu¨rich,Switzerland.NovelComputationalTechniquesinNM
2、RStructureDeterminationNuclearmagneticresonance(NMR)spectroscopyenablesthedeterminationofthree-.ChemicalShiftsandProteinStructuredimensionalproteinstructuresatatomicresolutionundernear-physiologicalconditionsin.NMRofParamagneticProteinssolution.Instructuralbiology,NMRcomplementsX-rayc
3、rystallography,whichprovidessimilarinformationonproteinsinsinglecrystals.IntroductionFortheNMRsamplepreparation,theproteinis21dissolvedatabout1mmolLconcentrationin0.5mLForabout25years,X-raydiffractioninsinglecrystalswasofwater.Theionicstrength,pH,temperature,andpossiblyuniqueinitsabili
4、tytodeterminethree-dimensional(3D)theconcentrationofadditivesmaythenbeadjusted,forstructuresofproteinsatatomicresolution.Thesituationexampletoensurenear-physiologicalconditionsordena-changedin1984withthecompletionofaproteinstructureturingconditions,andsoon.determinationbynuclearmagnet
5、icresonance(NMR)ThedemandsonNMRexperimentsformacromolecularspectroscopyinsolution,andtodayNMRisasecond,structuredeterminationaremetbymultidimensionalwidelyusedmethodforproteinstructuredetermination.InNMRathighpolarizingmagneticfields.Thekeyexperi-1990therewere109publicationsdescribingn
6、ovelX-ray11mentisH–HnuclearOverhausereffectspectroscopystructuresofproteinsandnucleicacids,and23newNMR(NOESY),whichenablesthemeasurementofproton–structures;in1998thecropofnewstructureswas747byX-protondistancesasinputforthestructurecalculation.raycrystallographyand125byNMR.Thisrapidgrow
7、thWithincreasingmolecularsizeandconcomitantincreaseofstructuralbiologyisexpectedtocontinueoreventoofthenumberofNMRpeaks,itbecomesmoreandmoreacceleratewiththeadventof‘structuralgenomics’.Aswellastheirindependentapplicationforproteinstructuredetermination,NMRspectroscopyandX-raydiffracti
8、onSam
