Structural interpretation of hydrogen exchange protection factors in proteins: characterization of the native state fluctuations of CI2.
Protection factors obtained from equilibrium hydrogen exchange experiments are an important source of structural information on both native and nonnative states of proteins. We present a method for determining ensembles of protein structures by using hydrogen exchange data as restraints in molecular dynamics simulations in conjunction with an empirical force-field. The method is applied to determine the ensemble of structures representing the native state of chymotrypsin inhibitor 2 (CI2), including the rare, large fluctuations responsible for hydrogen exchange.
Best
Robert B
RB
Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Vendruscolo
Michele
M
D002918:Chymotrypsin / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D003198:Computer Simulation; D041961:Deuterium Exchange Measurement / Q000379:methods*; D006801:Humans; D006859:Hydrogen / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D008956:Models, Chemical; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D010940:Plant Proteins; D017434:Protein Structure, Tertiary; D013816:Thermodynamics
D010455:Peptides; D010940:Plant Proteins; C093336:chymotrypsin inhibitor 2; D006859:Hydrogen; D002918:Chymotrypsin