The muscle M-band protein myomesin comprises a 36-nm long filament made of repetitive immunoglobulin–helix modules that can stretch to 2.5-fold this length, demonstrating substantial molecular elasticity

A Fukuzawa

A. C Edman

B. K Grove

E. J. M Speel

F Berkemeier

F Steiner

G. F Elliott

G. G Knappeis

H. T Pask

I Agarkova

I Matsubara

J. L Woodhead

John Trinick

L. C Yu

Larissa Tskhovrebova

M Yamaguchi

M. A Goldstein

M. G Price

N Pinotsis

P Bertoncini

P Luther

P. A Kenny

P. F. M Van der Ven

R Horowits

R Schoenauer

S Lange

T Hornemann

T. C Irving

U Vinkemeier

W. M. J Obermann

English

PubMed

Skeletal and cardiac muscles are remarkable biological machines that support and move our bodies and power the rhythmic work of our lungs and hearts. As well as producing active contractile force, muscles are also passively elastic, which is essential to their performance. The origins of both active contractile and passive elastic forces can be traced to the individual proteins that make up the highly ordered structure of muscle. In this Primer, we describe the organization of sarcomeres--the structural units that produce contraction--and the nature of the proteins that make muscle elastic. In particular, we focus on an elastic protein called myomesin, whose novel modular architecture helps explain elasticity

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Making muscle elastic: the structural basis of myomesin stretching.

Tskhovrebova Larissa

Trinick John

Public Library of Science (PLOS)

Making Muscle Elastic: The Structural Basis of Myomesin Stretching

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Making Muscle Elastic: The Structural Basis of Myomesin Stretching

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