Comparison of amino acid sequence of troponin I from different striated muscles.

Nature ·Vol. 271 ·No. 5640 ·1978-01-05 ·Pages 31-5

Wilkinson JM, Grand RJ

Abstract

The sequence of troponin I from fast and slow skeletal and cardiac muscle shows strong homology in the region which binds to actin and is responsible for inhibition of the actomyosin AT Pase. More differences are found in the N-terminal region which binds to troponin C.

MeSH Terms

Actins/metabolism Adenosine Triphosphatases/antagonists & inhibitors Amino Acid Sequence Animals Binding Sites Biological Evolution Chickens Muscle Proteins/metabolism Myocardium Phosphates/metabolism Protein Binding Protein Conformation Rabbits Structure-Activity Relationship Troponin/metabolism

Chemicals

Actins Muscle Proteins Phosphates Troponin Adenosine Triphosphatases

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Wilkinson J M

Grand R J

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/271031a0

Published

1978-01-05

Pages

31-5

Language

English

Region

England

NLM ID

0410462

Subset

External Links

PubMed source DOI: 10.1038/271031a0 View journal details

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Comparison of amino acid sequence of troponin I from different striated muscles.

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