X-ray diffraction of strained muscle fibers in rigor.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 78 ·No. 9 ·1981-09-00 ·Pages 5559-63

Naylor GR, Podolsky RJ

Abstract

The effect of strain on the equatorial x-ray diffraction pattern of glycerinated rabbit psoas fibers was studied in the rigor (ATP free) state. Strains between 30 and 100 A per half sarcomere, measured directly by laser diffraction, did not change the intensity ratio, (10)/ . (11). Because the intensity ratio depends on the distribution of mass within the myofilament lattice, the negative result indicates that strain does not change the angle of attachment of the subfragment 1 (S1) moiety of the myosin molecule to the actin filament. The effect of strain on the ordering of the actin filaments also was considered and judged to be negligible.

MeSH Terms

Actomyosin Animals Cytoskeleton/ultrastructure Muscle Contraction Muscles/ultrastructure Rabbits Rigor Mortis X-Ray Diffraction

Chemicals

Actomyosin

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Naylor G R

Podolsky R J

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20 references, click to expand

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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.78.9.5559

Published

1981-09-00

Pages

5559-63

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC348786

Subset

External Links

PubMed source DOI: 10.1073/pnas.78.9.5559 PMC Full Text View journal details

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X-ray diffraction of strained muscle fibers in rigor.

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