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1、NMRSpectroscopyforSecondaryarticleMonitoringMolecularArticleContents.IntroductionDynamicsinSolution.IsotopicEnrichmentforRelaxationStudies.TheoryofRelaxationAndrewLLee,UniversityofPennsylvania,Philadelphia,Pennsylvania,USA.NMRRelaxationMeasurements.InterpretationofRelaxationParame
2、tersAJoshuaWand,UniversityofPennsylvania,Philadelphia,Pennsylvania,USA.BackboneDynamicsinProteins.Side-chainDynamicsinProteinsBiologicalmacromoleculesexhibitawiderangeofdynamicmotions.Analysisofrelaxation.ExpandingtheRangeofDynamicInformationratesofNMRsignalsallowsthesemotionstobe
3、characterizedthroughouta.DynamicsandEntropymacromoleculeatanatomiclevelofdetail.Introductiondynamicsofthebackboneofaprotein,analysisofamide15NrelaxationratesisthemostconvenientapproachandNuclearmagneticresonance(NMR)spectroscopyisa15requiresuniformNenrichmentoftheprotein.Foraccess
4、powerfultoolforcharacterizingstructureanddynamicsin13toproteinside-chaindynamics,variousapproachestoCbiologicalmacromolecules.Althoughothertechniques,2andHrelaxationrelyonuniformorspecificlabellingsuchasX-raycrystallography,canalsodeterminehigh-patterns,usuallyattainableinabacteria
5、lexpressionresolutionstructures,NMRisuniquelysuitedtothetask13system.InthecaseofCrelaxationofside-chainmethylofcharacterizingdynamicmotionswithinamolecule,groupsinproteins,thedesiredlabellingschemecanbeprimarilyfortworeasons.First,NMR-activenucleiare13obtainedfrombacterialgrowthon
6、mediawith[3-C]pyr-distributednaturally(orcanbeconvenientlyplaced)uvateasthesolecarbonsource.Someapproachesexploitthroughoutthebiomolecule,sothatmotionscanbethepropertiesofrandomfractionalisotopicincorpora-individuallymonitoredwithoutchemicallyperturbingtion,whereasotherstakeadvant
7、ageofbiosyntheticthemolecule.Second,thedetailsofmolecularmotionpathwaysinEscherichiacolitoyieldspecificpatternsofdirectlydeterminetherateatwhichnuclearmagnetizationisotopicenrichment.returnstoequilibrium.HeteronuclearNMR-basedstudiesofmotionalflexibilitywerepioneeredinapplicationsto
8、proteins.ApplicationstoRNAandDNAa
