期刊
PHYSICAL REVIEW LETTERS
卷 125, 期 5, 页码 -出版社
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.125.058001
关键词
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资金
- National Science Foundation [1715627]
- Israel Science Foundation [550/15, 453/17]
- United States-Israel Binational Science Foundation [2016696]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1715627] Funding Source: National Science Foundation
Glassy, nonexponential relaxations in globular proteins are typically attributed to conformational behaviors that are missing from intrinsically disordered proteins. Yet, we show that single molecules of a disordered-protein construct display two signatures of glassy dynamics, logarithmic relaxations and a Kovacs memory effect, in response to changes in applied tension. We attribute this to the presence of multiple independent local structures in the chain, which we corroborate with a model that correctly predicts the force dependence of the relaxation. The mechanism established here likely applies to other disordered proteins.
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