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Journal article

Gly126Arg substitution causes anomalous behaviour of α-skeletal and β-smooth tropomyosins during the ATPase cycle.

Abstract:

To investigate how TM stabilization induced by the Gly126Arg mutation in skeletal α-TM or in smooth muscle β-TM affects the flexibility of TMs and their position on troponin-free thin filaments, we labelled the recombinant wild type and mutant TMs with 5-IAF and F-actin with FITC-phalloidin, incorporated them into ghost muscle fibres and studied polarized fluorescence at different stages of the ATPase cycle. It has been shown that in the myosin- and troponin-free filaments the Gly126Arg mutat...

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Publication status:
Published

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Publisher copy:
10.1016/j.abb.2013.12.016

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Institution:
University of Oxford
Department:
Oxford, MSD, RDM, Cardiovascular Medicine, BHF Centre of Research Excellence
Role:
Author
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Journal:
Archives of biochemistry and biophysics
Volume:
543
Pages:
57-66
Publication date:
2014-02-05
DOI:
EISSN:
1096-0384
ISSN:
0003-9861
URN:
uuid:53aac303-889d-445c-833c-28a6aac288ef
Source identifiers:
445866
Local pid:
pubs:445866

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