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Dynamic Prestress in a Globular Protein 英文参考文献
DynamicPrestressinaGlobularProtein
ScottA.Edwards1,JohannesWagner1,2,FraukeGra¨ter1,2
*
1CAS-MPGPartnerInstituteandKeyLaboratoryforComputationalBiology,Shanghai,China,2HeidelbergInstituteforTheoreticalStudies,Heidelberg,Germany
Abstract
Aproteinatequilibriumiscommonlythoughtofasafullyrelaxedstructure,withtheintra-molecularinteractionsshowing
fluctuationsaroundtheirenergyminimum.Incontrast,herewefinddirectevidenceforaproteinasamoleculartensegrity
structure, comprising a balance of tensed and compressed interactions, a concept that has been put forward for
macroscopicstructures.Wequantifiedthedistributionofinter-residueprestressinubiquitinandimmunoglobulinfromall-
atommoleculardynamicssimulations.Thenetworkofhighlyfluctuatingyetsignificantinter-residueforcesinproteinsisa
consequence of the intrinsic frustration of a protein when sampling its rugged energy landscape. In beta sheets, this
balanceofforcesisfoundtocompresstheintra-strandhydrogenbonds.Weestimatethattheobservedmagnitudeofthis
pre-compressionisenoughtoinducesignificantchangesinthehydrogenbondlifetimes;thus,prestress,whichcanbeas
highasafew100pN,canbeconsideredakeyfactorindeterminingtheunfoldingkineticsandpathwayofproteinsunder
force.Strongpre-tensionincertainsaltbridgesontheotherhandisconnectedtothethermodynamicstabilityofubiquitin.
Effectiveforceprofilesbetweensomeside-chainsrevealthesignatureofmultiple,distinctconformationalstates,andsuch
static disorder could be one factor explaining the growing body of experiments revealing non-exponential unfolding
kineticsofproteins.Thedesignofprestressdistributionsinengineeringproteinspromisestobeanewtoolfortailoringthe
mechanicalpropertiesofmade-to-ordernanomaterials.
Citation:EdwardsSA,WagnerJ,Gra¨ter F(2012)DynamicPrestressinaGlobularProtein.PLoSComputBiol8(5):e1002509.doi:10.1371/journal.pcbi.1002509
Editor:RuthNussinov,NationalCancerInstitute,UnitedStatesofAmericaandTelAvivUniversity,Israel,UnitedStatesofAmerica
ReceivedSeptember22,2011;AcceptedMarch21,2012;P
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