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PMID: 7787114 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Millisecond time resolution electron cryo-microscopy of the M-ATP transient kinetic state of the acto-myosin ATPase.

Biophysical journal ·Vol. 68 ·No. 4 Suppl ·1995-04-00 ·Pages 87S-91S

Walker M, Trinick J, White H

Abstract

The structure of the AM-ATP transient kinetic state of the acto-myosin ATPase cycle has been examined by electron microscopy using frozen-hydrated specimens prepared in low ionic strength. By spraying grids layered with the acto-S1 complex with ATP immediately before freezing, it was possible to examine the structure of the ternary complex with a time resolution of 10 ms. Disordered binding of the S1 was observed, suggesting more than one attachment geometry. This could be due to the presence of more than one biochemical intermediate, or to a single intermediate binding in more than one conformation.

MeSH Terms
Adenosine Triphosphate/analogs & derivatives,metabolism Animals Biophysical Phenomena Biophysics Freezing Hydrolysis In Vitro Techniques Kinetics Microscopy, Electron Models, Biological Muscle Contraction/physiology Myosin Subfragments/metabolism,physiology,ultrastructure Myosins/metabolism,physiology,ultrastructure Osmolar Concentration Swine ortho-Aminobenzoates
Chemicals
Myosin Subfragments ortho-Aminobenzoates 3'-O-(N-methylanthraniloyl) ATP Adenosine Triphosphate Myosins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Walker M
Muscle and Collagen Group, Bristol University Veterinary School, Langford, United Kingdom.
Trinick J
White H
References (19)
19 references, click to expand
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1995-04-00
Pages
87S-91S
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1281881
Subset
IM
Grants
NHLBI NIH HHS · HL41776 · United States
External Links
PubMed source PMC Full Text View journal details
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