Abstract
Data of this study showed that αD-αE helices and the conserved interdomain linker are two interfaces essential not only for the self-association but also for the functional properties of rat HSC70. Self-association which is a conserved property of HSP70 seems to be important for the activity of these proteins.
Keywords: HSC70, Mutagenesis, Oligomerization, Ultracentrifugation, ATPase activity
Protein & Peptide Letters
Title: Analysis of Monomeric Mutants of HSC70: A Possible Relationship Between Oligomerization and Functional Properties
Volume: 14 Issue: 8
Author(s): Mouna Amor-Mahjoub, Nathalie Gomez-Vrielyunck, Jean Philippe Suppini, Benoit Fouchaq, Nadia Benaroudj and Moncef Ladjimi
Affiliation:
Keywords: HSC70, Mutagenesis, Oligomerization, Ultracentrifugation, ATPase activity
Abstract: Data of this study showed that αD-αE helices and the conserved interdomain linker are two interfaces essential not only for the self-association but also for the functional properties of rat HSC70. Self-association which is a conserved property of HSP70 seems to be important for the activity of these proteins.
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Cite this article as:
Mouna Amor-Mahjoub , Nathalie Gomez-Vrielyunck , Jean Philippe Suppini , Benoit Fouchaq , Nadia Benaroudj and Moncef Ladjimi , Analysis of Monomeric Mutants of HSC70: A Possible Relationship Between Oligomerization and Functional Properties, Protein & Peptide Letters 2007; 14 (8) . https://dx.doi.org/10.2174/092986607781483624
DOI https://dx.doi.org/10.2174/092986607781483624 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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