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  The molecular basis of cross-bridge function

Holmes, K. C. (2005). The molecular basis of cross-bridge function. In H. Sugi (Ed.), Sliding filament mechanism in muscle contraction (pp. 13-23). New York: Springer.

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AdvExpMedBiol_565_2005_13.pdf (Any fulltext), 572KB
 
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AdvExpMedBiol_565_2005_359.pdf (Supplementary material), 696KB
 
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 Creators:
Holmes, Kenneth C.1, Author           
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1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: 8. Conclusion: Three of the four states anticipated by the Lymn-Taylor cross-bridge cycle are now known in atomic detail. The “unbound” states, which are more easily available to protein crystallographic analysis, have yielded most information. The connections between ATP binding and the conformation of the myosin cross-bridge in solution are well understood. Besides being an ATPase the myosin “head” has two essential functions: a shape change induced by product release that drives contraction; a large change of affinity for actin induced by binding ATP. X-ray crystallography, in conjunction with electron microscopy has recently yielded an explanation of both these phenomena in molecular terms. The detailed structures of the actin bound states are gradually becoming available by combining crystal structures analysis with high-resolution electron microscopy. However, the structure of the ephemeral strong binding at the beginning of the power stroke can at present only be inferred.

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Language(s): eng - English
 Dates: 2005
 Publication Status: Issued
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Sliding filament mechanism in muscle contraction
Source Genre: Book
 Creator(s):
Sugi, Haruo1, Editor
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1 Teiko University, ou_persistent22            
Publ. Info: New York : Springer
Pages: - Volume / Issue: 565 Sequence Number: - Start / End Page: 13 - 23 Identifier: ISBN: 978-0-387-24989-6
URI: http://link.springer.com/book/10.1007/b106476

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Title: Advances in Experimental Medicine and Biology
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Publ. Info: New York : Springer
Pages: - Volume / Issue: 565 Sequence Number: - Start / End Page: - Identifier: ISSN: 0065-2598
URI: http://link.springer.com/bookseries/5584