NDLI: Using optical tweezers to relate the chemical and mechanical cross-bridge cycles.

Content Provider	PubMed Central
Author	Steffen, Walter Sleep, John
Abstract	In most current models of muscle contraction there are two translational steps, the working stroke, whereby an attached myosin cross-bridge moves relative to the actin filament, and the repriming step, in which the cross-bridge returns to its original orientation. The development of single molecule methods has allowed a more detailed investigation of the relationship of these mechanical steps to the underlying biochemistry. In the normal adenosine triphosphate cycle, myosin.adenosine diphosphate.phosphate (M.ADP.Pi) binds to actin and moves it by ca. 5 nm on average before the formation of the end product, the rigor actomyosin state. All the other product-like intermediate states tested were found to give no net movement indicating that M.ADP.Pi alone binds in a pre-force state.Myosin states with bound, unhydrolysed nucleoside triphosphates also give no net movement, indicating that these must also bind in a post-force conformation and that the repriming, post- to pre-transition during the forward cycle must take place while the myosin is dissociated from actin. These observations fit in well with the structural model in which the working stroke is aligned to the opening of the switch 2 element of the ATPase site.
Related Links	http://dx.doi.org/10.1098/rstb.2004.1558
Ending Page	1865
Page Count	9
Starting Page	1857
File Format	PDF
ISSN	09628436
e-ISSN	14712970
Journal	Philosophical Transactions of the Royal Society B: Biological Sciences
Issue Number	1452
Volume Number	359
Language	English
Publisher Date	2004-12-29
Access Restriction	Open
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Agricultural and Biological Sciences(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry, Genetics and Molecular Biology Agricultural and Biological Sciences

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