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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

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1437-4315
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Volume 381, Issue 9-10

Issues

Molecular Basis for Interactions of the DnaK Chaperone with Substrates

Matthias P. Mayer / Stefan Rüdiger / Bernd Bukau
Published Online: 2005-07-05 | DOI: https://doi.org/10.1515/BC.2000.109

Abstract

Hsp70 chaperones assist a large variety of protein folding processes in the cell by transient association with short peptide segments of proteins. The substrate binding and release cycle is driven by the switching between the low affinity ATP bound state and the high affinity ADP bound state of Hsp70. Considerable progress has been made recently by the identification of in vivo substrates for the Escherichia coli homolog, DnaK, and the molecular mechanisms which govern the DnaK-substrate interactions. Here we review the processes that generate DnaK substrates in vivo and the properties of these substrates, and we describe insights gained from structural and kinetic analysis of DnaK-substrate interaction.

About the article

Published Online: 2005-07-05

Published in Print: 2000-09-13


Citation Information: Biological Chemistry, Volume 381, Issue 9-10, Pages 877–885, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2000.109.

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