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Journal Article

Single-protein force spectroscopy: Sequence dependence

MPS-Authors
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Lee,  N.
MPI for Polymer Research, Max Planck Society;

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Vilgis,  Thomas A.
MPI for Polymer Research, Max Planck Society;

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Citation

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


Cite as: http://hdl.handle.net/11858/00-001M-0000-000F-667B-4
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.