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PMID: 2928326 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

On the origin and transmission of force in actomyosin subfragment 1.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 86 ·No. 7 ·1989-04-00 ·Pages 2204-8

Botts J, Thomason JF, Morales MF

Abstract

A proximity map showing the three-dimensional arrangement of 12 chemically defined points in actomyosin subfragment 1 is developed and roughly correlated with published electron microscope reconstruction of others. Several additional points and topological relationships in the primary polypeptide chain folding are assimilated into this model. Certain crosslinkings and distance change observations are interpreted as indicators of transmission of force/displacement between the nucleotide-binding and an actin-binding site--i.e., as indications of how energy is transduced in this system.

MeSH Terms
Microscopy, Electron/methods Models, Theoretical Myosin Subfragments Myosins/metabolism Peptide Fragments/metabolism Protein Conformation
Chemicals
Myosin Subfragments Peptide Fragments Myosins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Botts J
Cardiovascular Research Institute, University of California, San Francisco 94143.
Thomason J F
Morales M F
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.86.7.2204
Published
1989-04-00
Pages
2204-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC286880
Subset
IM
Grants
NHLBI NIH HHS · HL-16683 · United States
External Links
PubMed source DOI: 10.1073/pnas.86.7.2204 PMC Full Text View journal details
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