Elasticity and unfolding of single molecules of the giant muscle protein titin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-05

AUTHORS

L Tskhovrebova, J Trinick, J A Sleep, R M Simmons

ABSTRACT

The giant muscle protein titin, also called connectin, is responsible for the elasticity of relaxed striated muscle, as well as acting as the molecular scaffold for thick-filament formation. The titin molecule consists largely of tandem domains of the immunoglobulin and fibronectin-III types, together with specialized binding regions and a putative elastic region, the PEVK domain. We have done mechanical experiments on single molecules of titin to determine their visco-elastic properties, using an optical-tweezers technique. On a fast (0.1s) timescale titin is elastic and force-extension data can be fitted with standard random-coil polymer models, showing that there are two main sources of elasticity: one deriving from the entropy of straightening the molecule; the other consistent with extension of the polypeptide chain in the PEVK region. On a slower timescale and above a certain force threshold, the molecule displays stress-relaxation, which occurs in rapid steps of a few piconewtons, corresponding to yielding of internal structures by about 20 nm. This stress-relaxation probably derives from unfolding of immunoglobulin and fibronectin domains. More... »

PAGES

308-312

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/387308a0

DOI

http://dx.doi.org/10.1038/387308a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1012750390

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9153398


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