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- W1966251133 abstract "We report the first measurement of the reversible unfolding of protein molecules. The molecules are confined between a flat plate and a 10 μ m sphere, and we measure the displacement of the sphere caused by the unfolding of the molecules in denaturing agents. In the case of bovine serum albumin, this mechanical size of the protein increases by 9 nm (a doubling of the folded dimensions) in strong denaturants. The present technique measures a size which is the maximum extent of the molecules, and is thus complementary to other existing methods which measure a radius of gyration. It gives access to the dynamics of conformational changes over time scales from milliseconds to minutes." @default.
- W1966251133 created "2016-06-24" @default.
- W1966251133 creator A5085646546 @default.
- W1966251133 date "1996-09-10" @default.
- W1966251133 modified "2023-10-17" @default.
- W1966251133 title "Mechanical measurement of the unfolding of a protein" @default.
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- W1966251133 doi "https://doi.org/10.1209/epl/i1996-00163-6" @default.
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