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dc.contributor.author Xu, Y
dc.contributor.author Schmitt, S
dc.contributor.author Tang, L
dc.contributor.author Jakob, U
dc.contributor.author Fitzgerald, MC
dc.coverage.spatial United States
dc.date.accessioned 2011-06-21T17:22:10Z
dc.date.issued 2010-02-16
dc.identifier http://www.ncbi.nlm.nih.gov/pubmed/20073505
dc.identifier.citation Biochemistry, 2010, 49 (6), pp. 1346 - 1353
dc.identifier.uri http://hdl.handle.net/10161/4016
dc.description.abstract Molecular chaperones are a highly diverse group of proteins that recognize and bind unfolded proteins to facilitate protein folding and prevent nonspecific protein aggregation. The mechanisms by which chaperones bind their protein substrates have been studied for decades. However, there are few reports about the affinity of molecular chaperones for their unfolded protein substrates. Thus, little is known about the relative binding affinities of different chaperones and about the relative binding affinities of chaperones for different unfolded protein substrates. Here we describe the application of SUPREX (stability of unpurified proteins from rates of H-D exchange), an H-D exchange and MALDI-based technique, in studying the binding interaction between the molecular chaperone Hsp33 and four different unfolded protein substrates, including citrate synthase, lactate dehydrogenase, malate dehydrogenase, and aldolase. The results of our studies suggest that the cooperativity of the Hsp33 folding-unfolding reaction increases upon binding with denatured protein substrates. This is consistent with the burial of significant hydrophobic surface area in Hsp33 when it interacts with its substrate proteins. The SUPREX-derived K(d) values for Hsp33 complexes with four different substrates were all found to be within the range of 3-300 nM.
dc.format.extent 1346 - 1353
dc.language ENG
dc.language.iso en_US en_US
dc.relation.ispartof Biochemistry
dc.relation.isversionof 10.1021/bi902010t
dc.subject Animals
dc.subject Citrate (si)-Synthase
dc.subject Escherichia coli Proteins
dc.subject Fructose-Bisphosphate Aldolase
dc.subject Heat-Shock Proteins
dc.subject L-Lactate Dehydrogenase
dc.subject Malate Dehydrogenase
dc.subject Molecular Chaperones
dc.subject Protein Binding
dc.subject Protein Folding
dc.subject Rabbits
dc.subject Substrate Specificity
dc.subject Swine
dc.subject Thermodynamics
dc.title Thermodynamic analysis of a molecular chaperone binding to unfolded protein substrates.
dc.title.alternative en_US
dc.type Journal Article
dc.description.version Version of Record en_US
duke.date.pubdate 2010-2-16 en_US
duke.description.endpage 1353 en_US
duke.description.issue 6 en_US
duke.description.startpage 1346 en_US
duke.description.volume 49 en_US
dc.relation.journal Biochemistry en_US
pubs.author-url http://www.ncbi.nlm.nih.gov/pubmed/20073505
pubs.issue 6
pubs.organisational-group /Duke
pubs.organisational-group /Duke/School of Medicine
pubs.organisational-group /Duke/School of Medicine/Basic Science Departments
pubs.organisational-group /Duke/School of Medicine/Basic Science Departments/Biochemistry
pubs.organisational-group /Duke/Trinity College of Arts & Sciences
pubs.organisational-group /Duke/Trinity College of Arts & Sciences/Chemistry
pubs.publication-status Published
pubs.volume 49
dc.identifier.eissn 1520-4995

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