Single-protein force spectroscopy: Sequence dependence

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2002 EDP Sciences
, , Citation N. Lee and T. A. Vilgis 2002 EPL 57 817 DOI 10.1209/epl/i2002-00584-7

0295-5075/57/6/817

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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10.1209/epl/i2002-00584-7