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• W1998032049 abstract "The alpha-helix containing the thiols, SH1 (Cys-707) and SH2 (Cys-697), has been proposed to be one of the structural elements responsible for the transduction of conformational changes in the myosin head (subfragment-1 (S1)). Previous studies, using a method that isolated and measured the rate of the SH1-SH2 cross-linking step, showed that this helix undergoes ligand-induced conformational changes. However, because of long incubation times required for the formation of the transition state complexes (S1.ADP.BeF(x), S1.ADP.AlF(4)-, and S1.ADP.V(i)), this method could not be used to determine the cross-linking rate constants for such states. In this study, kinetic data from the SH1-SH2 cross-linking reaction were analyzed by computational methods to extract rate constants for the two-step mechanism. For S1.ADP.BeF(x), the results obtained were similar to those for S1.ATPgammaS. For reactions involving S1.ADP.AlF(4)- and S1.ADP.V(i), the first step (SH1 modification) is rate limiting; consequently, only lower limits could be established for the rate constants of the cross-linking step. Nevertheless, these results show that the cross-linking rate constants in the transition state complexes are increased at least 20-fold for all the reagents, including the shortest one, compared with nucleotide-free S1. Thus, the SH1-SH2 helix appears to be destabilized in the post-hydrolysis state." @default.
• W1998032049 created "2016-06-24" @default.
• W1998032049 creator A5038398169 @default.
• W1998032049 creator A5044907200 @default.
• W1998032049 creator A5061217668 @default.
• W1998032049 date "2002-11-01" @default.
• W1998032049 modified "2023-10-09" @default.
• W1998032049 title "Conformational Dynamics of the SH1-SH2 Helix in the Transition States of Myosin Subfragment-1" @default.
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• W1998032049 doi "https://doi.org/10.1016/s0006-3495(02)75283-1" @default.
• W1998032049 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1302358" @default.
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