The myosin head can bind two actin monomers.
The myosin head can bind two actin monomers.
复制标题
肌球蛋白头可以结合两个肌动蛋白单体。
DOI:
10.1016/0006-291x(91)91990-t
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发表时间:
1991
影响因子:
3.1
通讯作者:
J. Borejdo
中科院分区:
文献类型:
--
作者:
O. Andreev;J. Borejdo
Force impulse is thought to be generated in muscle when myosin head (S-1), while weakly bound to actin filament, undergoes orientational change to form a strong (rigor) bond with actin. There is ample evidence that this bond involves interaction of 1 myosin head with 1 actin monomer. However, X-ray diffraction data of muscle decorated with S-1, as well as recently proposed model of the thin filaments, suggested that each S-1 molecule interacted with two actin monomers. We reinvestigated this controversy and found that the stoichiometry of acto-S-1 bond depended on the relative amounts of actin and myosin present during titrations: when increasing amounts of actin were added to a fixed amount of S-1 (i.e. when myosin heads were initially in excess over actin), the saturating stoichiometry was 1 mol of S-1 per 1 mol of actin. However, when increasing amounts of S-1 were added slowly to a fixed amount of F-actin (i.e. when actin was initially in excess over S-1), the stoichiometry at saturation was 1 mol of S-1 per 2 mols of actin. The ability of S-1 to bind either one or two actin monomers suggests a way that force could be generated during muscle contraction.
影响因子:
2.9
作者:
Botts,J;Muhlrad,A;Takashi,R;Morales,MF
通讯作者:
Morales,MF
影响因子:
2.9
作者:
Lehrer,SS;Ishii,Y
通讯作者:
Ishii,Y
影响因子:
3.4
作者:
Stein,LA;Harwalkar,VA
通讯作者:
Harwalkar,VA