Protein structural transitions and their functional role

Author:

Karplus Martin12,Gao Yi Qin2,Ma Jianpeng3,van der Vaart Arjan12,Yang Wei2

Affiliation:

1. Laboratoire de Chimie Biophysique, ISIS, Université Louis Pasteur, 67000 Strasbourg, France

2. Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA ()

3. Department of Biochemistry, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA

Abstract

Living cells are a collection of molecular machines which carry out many of the functions essential for the cell's existence, differentiation and reproduction. Most, though not all, of these machines are made up of proteins. Because of their complexity, an understanding of how they work requires a synergistic combination of experimental and theoretical studies. In this paper we outline our studies of two such protein machines. One is GroEL, the chaperone from Escherichia coli , which aids in protein folding; the other is F 1 –ATPase, a motor protein which synthesizes and hydrolyses ATP.

Publisher

The Royal Society

Subject

General Physics and Astronomy,General Engineering,General Mathematics

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