[Estimation of the distance between sulfhydryl groups S1 and specific binding centers for divalent metal ions in myosin]

Autor: G G, Charkviani, A V, Kulikov, T M, Eristavi, Z O, Dzhaparidze
Rok vydání: 1981
Předmět:
Zdroj: Biofizika. 26(5)
ISSN: 0006-3029
Popis: Interlocation of sulfhydryl groups S1 and corresponding divalent ions binding sites in myosin has been studied. S1-SH groups were labelled with iodacetamide spin labels and their saturation curves were measured in the presence of Ca2+ and Mn2+. The spin-lattice relaxation rates 1/T1 of labels were calculated from saturation curves and according to their changes caused by replacing Ca2+ by Mn2+ the distance between sulfhydryl groups S1 and divalent ions binding sites were estimated to be 45 +/- 2.5 A. The addition of ATP to this system has not changed the character of interaction. An analysis of saturation curves measured within temperature range 20-100 K suggests that two myosin subfragments J differ in conformation at least in the range where S1-SH groups are located.
Databáze: OpenAIRE