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  γ-amido-ATP stabilizes a high-fluorescence state of myosin subfragment 1

Wray, J., & Jahn, W. (2002). γ-amido-ATP stabilizes a high-fluorescence state of myosin subfragment 1. FEBS Letters, 518(1), 97-100. doi:10.1016/S0014-5793(02)02654-6.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-7D94-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-7D95-F
Genre: Journal Article
Alternative Title : Gamma-amido-ATP stabilizes a high-fluorescence state of myosin subfragment 1

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FEBSLett_518_2002_97.pdf (Any fulltext), 111KB
 
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 Creators:
Wray, John1, Author              
Jahn, Werner1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: γ-amido-adenosine 5′-triphosphate; Myosin; Actomyosin; Tryptophan fluorescence
 Abstract: On binding to myosin subfragment 1 (S1), the gamma-amido derivative of ATP (ATPgammaNH2), an isomer of adenosine 5'-[beta,gamma-imido]-triphosphate (AMPPNP), induces a larger increase in the intrinsic (tryptophan) fluorescence than is seen with ATP. A binding constant of 1.7x10(7) M(-1) was measured for ATPgammaNH2, compared to 2.1-2.4x10(7) M(-1) for AMPPNP. ATPgammaNH2 was hydrolyzed only very slowly by S1. ATPgammaNH2 appears to stabilize the 'closed' conformation of S1, and does so without cleavage of the beta-gamma phosphate bond. The dissociation of actin-S1 by ATPgammaNH2 and that of S1.ATPgammaNH2 by actin are both strikingly slow.

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Language(s): eng - English
 Dates: 2002-03-252002-02-132002-03-252002-04-102002-05-08
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
 Creator(s):
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 518 (1) Sequence Number: - Start / End Page: 97 - 100 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501