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1、SolidStateNMRforStudyingMembraneProteinsANTHONYWATTSBiomembraneStructureUnit,DepartmentofBiochemistry,UniversityofOxford,SouthParksRoad,Oxford,OX13QU,UK,Phone:+441865275268,Fax:+441865275234/275259,E-mail:anthony.watts@bioch.ox.ac.ukAbstractSolidstateNMRisnow
2、establishedasamethodforresolvingstructuralinformationforlargebiomolecularcomplexessuchasmembrane-embeddedproteins.Inprinciple,thereisnomolecularweightlimittotheuseoftheapproach,althoughthecomplexityandvolumeofdataisstilloutsidecompleteassignmentandstructurald
3、eterminationsforanylarge(Mr>~40k)complex,unlessspecificmethodsareusedtoreducetheinformationcontent.Suchmethodsincludespecificresiduetypelabelling,labellingofputativesegmentsofaprotein,probingligandbindingsiteswithlabelledligands,orexaminationofcomplexesmadeup
4、ofsmaller,manageableunits,suchasoligomericionchannels.Labellingpossibilitiesoftenfollowmodelsfromabioinformaticsapproach.Inallcases,andincommonwithmostmembranestudies,samplepreparationisvital,andthisactivityalonecantakeconsider-ableeffortbeforeNMRcanbeapplied
5、–peptideorproteinproduction(synthesisorexpression)followedbyreconstitutionintobilayersand/orchemicalsynthesis,andthenresolutionofsuitablesamplegeometry,isstilltechnicallychallenging.Asexperienceisgainedinthefield,thisdevelop-menttimeshoulddecrease.Here,abrief
6、overviewoftheuseofsolidstateNMRformembraneproteinstructuraldeterminationswillbepresented.Keywords:SolidstateNMR,biomembranes,ionchannels,GPCR,drug-receptorinteractions,proteinstructure.45G.Pifat-Mrzljak(ed.),SupramolecularStructureandFunction9,45–73.©2007Spri
7、nger.46AnthonyWatts1.INTRODUCTIONFromthe~35,000atomicresolutionstructuresintheproteindatabase,some6,000haveuniquefoldsbutonly~40areofmembraneproteins.Thislackofinformationaboutmembraneproteinswouldnotbesoimportantifpredictionmethodsweremoreeffective.However,s
8、incethisdirectdataisnotavailableinthequantitydesired,itisoftensuggestedthatmembraneproteinspresentthelastremainingmajorchallengeinstructuralbiology.Thelackofstructuraldatadoesnotparallelt
