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  Mobile segments in rabbit skeletal muscle F-actin detected by 1H nuclear magnetic resonance spectroscopy

Slósarek, G., Heintz, D., & Kalbitzer, H. R. (1994). Mobile segments in rabbit skeletal muscle F-actin detected by 1H nuclear magnetic resonance spectroscopy. FEBS Letters, 351(3), 405-410. doi:10.1016/0014-5793(94)00894-9.

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FEBSLett_351_1994_405.pdf (Any fulltext), 484KB
 
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 Creators:
Slósarek, Genowefa, Author
Heintz, Daniela, Author
Kalbitzer, Hans Robert1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: Actin; Mobility; 1H NMR; Muscle; G-actin, globular actin; F-actin, filamentous actin
 Abstract: Polymerization of actin by increasing the ionic strength leads to a quenching of almost all 1H NMR signals. Surprisingly, distinct signals with relatively small line widths can still be observed in actin filaments (F-actin) indicating the existence of mobile, NMR visible residues in the macromolecular structure. The intensity of the F-actin spectrum is much reduced if one replaces Mg2+ with Ca2+, and a moderate reduction of the signal intensity can also be obtained by increasing the ionic strength. These results can be explained in a two-state model of the actin promoters with a M- (mobile) state and a I- (immobile) state in equilibrium. In the M-state a number of residues in the actin promoter are mobile and give rise to observable NMR signals. This equilibrium is shifted towards the I-state specifically by replacing Mg2+ with Ca(2+)-ions and unspecifically by addition of monovalent ions such as K+. The binding of phalloidin to its high-affinity site in the filaments does not influence the equilibrium between M- and I-state. Phalloidin itself is completely immobilized in F-actin, its exchange with the solvent being slow on the NMR time scale.

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Language(s): eng - English
 Dates: 1994-07-221994-08-052001-10-181994-09-12
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 665176
DOI: 10.1016/0014-5793(94)00894-9
URI: https://www.ncbi.nlm.nih.gov/pubmed/8082804
Other: 6909
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 351 (3) Sequence Number: - Start / End Page: 405 - 410 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501