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1、NuclearMagneticSecondaryarticleResonanceSpectroscopyofArticleContents.IntroductionProteins.NMRStructureDeterminationofProteins.NewExperimentalApproachesforHigh-molecularMassSystemsKurtWu¨thrich,SwissFederalInstituteofTechnology(ETH),Zu¨rich,Switzerland.NovelComputationalTechniquesinNMRSt
2、ructureDeterminationNuclearmagneticresonance(NMR)spectroscopyenablesthedeterminationofthree-.ChemicalShiftsandProteinStructuredimensionalproteinstructuresatatomicresolutionundernear-physiologicalconditionsin.NMRofParamagneticProteinssolution.Instructuralbiology,NMRcomplementsX-raycrystal
3、lography,whichprovidessimilarinformationonproteinsinsinglecrystals.IntroductionFortheNMRsamplepreparation,theproteinis21dissolvedatabout1mmolLconcentrationin0.5mLForabout25years,X-raydiffractioninsinglecrystalswasofwater.Theionicstrength,pH,temperature,andpossiblyuniqueinitsabilitytodeter
4、minethree-dimensional(3D)theconcentrationofadditivesmaythenbeadjusted,forstructuresofproteinsatatomicresolution.Thesituationexampletoensurenear-physiologicalconditionsordena-changedin1984withthecompletionofaproteinstructureturingconditions,andsoon.determinationbynuclearmagneticresonance(
5、NMR)ThedemandsonNMRexperimentsformacromolecularspectroscopyinsolution,andtodayNMRisasecond,structuredeterminationaremetbymultidimensionalwidelyusedmethodforproteinstructuredetermination.InNMRathighpolarizingmagneticfields.Thekeyexperi-1990therewere109publicationsdescribingnovelX-ray11ment
6、isH–HnuclearOverhausereffectspectroscopystructuresofproteinsandnucleicacids,and23newNMR(NOESY),whichenablesthemeasurementofproton–structures;in1998thecropofnewstructureswas747byX-protondistancesasinputforthestructurecalculation.raycrystallographyand125byNMR.ThisrapidgrowthWithincreasingmo
7、lecularsizeandconcomitantincreaseofstructuralbiologyisexpectedtocontinueoreventoofthenumberofNMRpeaks,itbecomesmoreandmoreacceleratewiththeadventof‘structuralgenomics’.Aswellastheirindependentapplicationforproteinstructuredetermination,NMRspectroscopyandX-raydiffractionSam
