English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  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.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-C16E-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-C178-0
Genre: Book Chapter

Files

show Files
hide Files
:
AdvExpMedBiol_565_2005_13.pdf (Any fulltext), 572KB
 
File Permalink:
-
Name:
AdvExpMedBiol_565_2005_13.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
AdvExpMedBiol_565_2005_359.pdf (Supplementary material), 696KB
 
File Permalink:
-
Name:
AdvExpMedBiol_565_2005_359.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
Description:
-

Creators

show
hide
 Creators:
Holmes, Kenneth C.1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

Content

show
hide
Free keywords: -
 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.

Details

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

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Sliding filament mechanism in muscle contraction
Source Genre: Book
 Creator(s):
Sugi, Haruo1, Editor
Affiliations:
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

Source 2

show
hide
Title: Advances in Experimental Medicine and Biology
Source Genre: Series
 Creator(s):
Affiliations:
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