Signatures of Hydrophobic Collapse in Extended Proteins Captured with Force Spectroscopy

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2007 May 2

PMID 17470816

Citations 39

Authors

Kirstin A Walther

Frauke Grater

Lorna Dougan

Carmen L Badilla

Bruce J Berne

Julio M Fernandez

Affiliations

Soon will be listed here.

Abstract

We unfold and extend single proteins at a high force and then linearly relax the force to probe their collapse mechanisms. We observe a large variability in the extent of their recoil. Although chain entropy makes a small contribution, we show that the observed variability results from hydrophobic interactions with randomly varying magnitude from protein to protein. This collapse mechanism is common to highly extended proteins, including nonfolding elastomeric proteins like PEVK from titin. Our observations explain the puzzling differences between the folding behavior of highly extended proteins, from those folding after chemical or thermal denaturation. Probing the collapse of highly extended proteins with force spectroscopy allows separation of the different driving forces in protein folding.

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