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Muscle contraction mechanism based on single molecule measurements
Single molecule measurements have shown that a muscle myosin step is driven by biased Brownian movement. Furthermore, they have also demonstrated that in response to strain in the backward direction a detached myosin head preferentially attaches to the forward direction due to an accelerated transit...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3521640/ https://www.ncbi.nlm.nih.gov/pubmed/23203295 http://dx.doi.org/10.1007/s10974-012-9332-7 |
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author | Yanagida, Toshio Ishii, Yoshiharu |
author_facet | Yanagida, Toshio Ishii, Yoshiharu |
author_sort | Yanagida, Toshio |
collection | PubMed |
description | Single molecule measurements have shown that a muscle myosin step is driven by biased Brownian movement. Furthermore, they have also demonstrated that in response to strain in the backward direction a detached myosin head preferentially attaches to the forward direction due to an accelerated transition from a weak binding to strong binding state. Because they are consistent with the original Huxley model for muscle contraction, we have built a model that describes macroscopic muscle characteristics based on these single molecule results. |
format | Online Article Text |
id | pubmed-3521640 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-35216402012-12-14 Muscle contraction mechanism based on single molecule measurements Yanagida, Toshio Ishii, Yoshiharu J Muscle Res Cell Motil Original Paper Single molecule measurements have shown that a muscle myosin step is driven by biased Brownian movement. Furthermore, they have also demonstrated that in response to strain in the backward direction a detached myosin head preferentially attaches to the forward direction due to an accelerated transition from a weak binding to strong binding state. Because they are consistent with the original Huxley model for muscle contraction, we have built a model that describes macroscopic muscle characteristics based on these single molecule results. Springer Netherlands 2012-12-01 2012 /pmc/articles/PMC3521640/ /pubmed/23203295 http://dx.doi.org/10.1007/s10974-012-9332-7 Text en © The Author(s) 2012 https://creativecommons.org/licenses/by/2.0/ Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited. |
spellingShingle | Original Paper Yanagida, Toshio Ishii, Yoshiharu Muscle contraction mechanism based on single molecule measurements |
title | Muscle contraction mechanism based on single molecule measurements |
title_full | Muscle contraction mechanism based on single molecule measurements |
title_fullStr | Muscle contraction mechanism based on single molecule measurements |
title_full_unstemmed | Muscle contraction mechanism based on single molecule measurements |
title_short | Muscle contraction mechanism based on single molecule measurements |
title_sort | muscle contraction mechanism based on single molecule measurements |
topic | Original Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3521640/ https://www.ncbi.nlm.nih.gov/pubmed/23203295 http://dx.doi.org/10.1007/s10974-012-9332-7 |
work_keys_str_mv | AT yanagidatoshio musclecontractionmechanismbasedonsinglemoleculemeasurements AT ishiiyoshiharu musclecontractionmechanismbasedonsinglemoleculemeasurements |