Protein structural transitions and their functional role
- 13 December 2004
- journal article
- review article
- Published by The Royal Society in Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences
- Vol. 363 (1827) , 331-356
- https://doi.org/10.1098/rsta.2004.1496
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.Keywords
This publication has 100 references indexed in Scilit:
- The energy landscape as a unifying theme in molecular sciencePhilosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences, 2004
- A Normal Mode Analysis of Structural Plasticity in the Biomolecular Motor F1-ATPaseJournal of Molecular Biology, 2004
- Protein-misfolding diseases: Getting out of shapeNature, 2002
- ATP-Bound States of GroEL Captured by Cryo-Electron MicroscopyPublished by Elsevier ,2001
- Protein Compactness Measured by Fluorescence Resonance Energy TransferJournal of Biological Chemistry, 2001
- A dynamic model for the allosteric mechanism of GroEL 1 1Edited by A. FershtJournal of Molecular Biology, 2000
- The Crystal Structure of a GroEL/Peptide ComplexCell, 1999
- Conformational States Bound by the Molecular Chaperones GroEL and SecB: A Hidden Unfolding (Annealing) ActivityJournal of Molecular Biology, 1996
- Targeted Molecular Dynamics Simulation of Conformational Change-Application to the T ↔ R Transition in InsulinMolecular Simulation, 1993
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983