4.5 Review Book Chapter

The Work of Titin Protein Folding as a Major Driver in Muscle Contraction

期刊

ANNUAL REVIEW OF PHYSIOLOGY, VOL 80
卷 80, 期 -, 页码 327-351

出版社

ANNUAL REVIEWS
DOI: 10.1146/annurev-physiol-021317-121254

关键词

muscle contraction; titin; protein folding; polymer physics; single molecule; force spectroscopy

资金

  1. US National Institutes of Health (NIH) [GM116122, HL061228]
  2. National Science Foundation [DBI-1252857]
  3. NIH [5F30HL129662]
  4. Fundacion Ramon Areces

向作者/读者索取更多资源

Single-molecule atomic force microscopy and magnetic tweezers experiments have demonstrated that titin immunoglobulin (Ig) domains are capable of folding against a pulling force, generating mechanical work that exceeds that produced by a myosin motor. We hypothesize that upon muscle activation, formation of actomyosin cross bridges reduces the force on titin, causing entropic recoil of the titin polymer and triggering the folding of the titin Ig domains. In the physiological force range of 4-15 pN under which titin operates in muscle, the folding contraction of a single Ig domain can generate 200% of the work of entropic recoil and occurs at forces that exceed the maximum stalling force of single myosin motors. Thus, titin operates like a mechanical battery, storing elastic energy efficiently by unfolding Ig domains and delivering the charge back by folding when the motors are activated during a contraction. We advance the hypothesis that titin folding and myosin activation act as inextricable partners during muscle contraction.

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