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PubMed · 15664887

Protein structural transitions and their functional role.

Martin Karplus·Yi Qin Gao·Jianpeng Ma·Arjan van der Vaart·Wei Yang
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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.

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Chaperonin 60Energy TransferModels, BiologicalModels, ChemicalModels, MolecularMolecular Motor ProteinsMotionProtein ConformationProtein FoldingProton-Translocating ATPasesStructure-Activity RelationshipJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.Review

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Martin Karplus, Yi Qin Gao, Jianpeng Ma, Arjan van der Vaart, Wei Yang. 2005-02-15. Protein structural transitions and their functional role.. https://doi.org/10.1098/rsta.2004.1496

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