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  Single-protein force spectroscopy: Sequence dependence

Lee, N., & Vilgis, T. A. (2002). Single-protein force spectroscopy: Sequence dependence. Europhysics Letters, 57(6), 817-823.

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 Creators:
Lee, N.1, Author              
Vilgis, Thomas A.1, Author              
Affiliations:
1MPI for Polymer Research, Max Planck Society, ou_1309545              

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 Abstract: We study the elastic properties of a single A/B copolymer chain with a specific sequence. We predict a rich structure in the force-extension relations which can be addressed to the sequence. The variational method is introduced to probe local minima on the path of stretching and releasing. At a given force, we find multiple configurations which are separated by energy barriers. A collapsed globular configuration consists of several domains which unravel cooperatively. Upon stretching, the unfolding path shows a stepwise pattern corresponding to the unfolding of each domain. While releasing, several cores can be created simultaneously in the middle of the chain resulting in a different path of collapse.

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Language(s): eng - English
 Dates: 2002-03
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: No review
 Identifiers: eDoc: 28529
ISI: 000174448700007
Other: P-02-99
 Degree: -

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Title: Europhysics Letters
  Alternative Title : Europhys. Lett.
Source Genre: Journal
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Pages: - Volume / Issue: 57 (6) Sequence Number: - Start / End Page: 817 - 823 Identifier: ISSN: 0295-5075