Are there two different binding sites for ATP on the myosin head, or only one that switches between two conformers?
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Biochemistry,Physiology
Link
http://link.springer.com/article/10.1007/s10974-017-9480-x/fulltext.html
Reference32 articles.
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2. Bagshaw CR, Eccleston JF, Eckstein F et al (1974) The magnesium ion-dependent adenosine triphosphatase of myosin. Two-step processes of adenosine triphosphate association and adenosine diphosphate dissociation. Biochem J 141:351–364
3. Barman TE, Travers F (1985) The rapid-flow-quench method in the study of fast reactions in biochemistry: extension to subzero conditions. Methods Biochem Anal 31:1–59
4. Barman TE, Hillaire D, Travers F (1983) Evidence for the two-step binding of ATP to myosin subfragment 1 by the rapid-flow-quench method. Biochem J 209:617–626
5. Biosca JA, Barman TE, Travers F (1984) Transient kinetics of the binding of ATP to actomyosin subfragment 1: evidence that the dissociation of actomyosin subfragment 1 by ATP leads to a new conformation of subfragment 1. BioChemistry 23:2428–2436
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