Geeves, Michael A. (2012) 4.13 Thin Filament Regulation. Comprehensive Biophysics, 4 (1). pp. 251-267. ISSN 978-0-12-374920-8. (doi:10.1016/B978-0-12-374920-8.00416-1) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:34208)
The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. | |
Official URL: http://dx.doi.org/10.1016/B978-0-12-374920-8.00416... |
Abstract
The review summarizes the current state of knowledge of the calcium regulation of striated muscle contraction via the thin filament proteins, tropomyosin and troponin. The description focuses on in vitro studies of the thin filament and covers structural, biochemical and dynamic aspects of the thin filament's response to calcium binding. A reductionist approach has allowed many of the transitions to be defined at the level of a single structural unit. Here an emphasis is placed on the co-operative nature of the structural and biochemical transitions of the thin filament and the allosteric relationship between calcium and myosin binding to the thin filament.
Item Type: | Article |
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DOI/Identification number: | 10.1016/B978-0-12-374920-8.00416-1 |
Uncontrolled keywords: | Actin; Allosteric; Calcium; Co-operativity; Coupled equilibria; E-F hand; Inhibitory peptide; Motility; Myosin; Persistence length; Signal peptide; Thin filament; Tropomyosin; Troponin |
Subjects: | Q Science |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Michael Geeves |
Date Deposited: | 06 Jun 2013 15:53 UTC |
Last Modified: | 05 Nov 2024 10:17 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/34208 (The current URI for this page, for reference purposes) |
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