[ASAP] Optimizing the First TPR Domain of the Human SPAG1 Protein Provides Insight into the HSP70 and HSP90 Binding Properties
Optimizing the First TPR Domain of the Human SPAG1 Protein Provides Insight into the HSP70 and HSP90 Binding Properties
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00052/20210319/images/medium/bi1c00052_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.1c00052
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Conformational heterogeneity in the Hsp70 chaperone-substrate ensemble identified from analysis of NMR-detected titration data
Conformational heterogeneity in the Hsp70 chaperone-substrate ensemble identified from analysis of NMR-detected titration data
Abstract
The Hsp70 chaperone system plays a critical role in cellular homeostasis by binding to client protein molecules. We have recently shown by methyl-TROSY NMR methods that the Escherichia coli Hsp70, DnaK, can form multiple bound complexes with a small client protein, hTRF1. In an effort to characterize the interactions further we report here the results of an NMR-based titration study of hTRF1 and DnaK, where both molecular components are monitored...
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09-18-2017 10:41 AM
[NMR paper] Conformational heterogeneity in the Hsp70 chaperone-substrate ensemble: identified from analysis of NMR-detected titration data.
Conformational heterogeneity in the Hsp70 chaperone-substrate ensemble: identified from analysis of NMR-detected titration data.
Related Articles Conformational heterogeneity in the Hsp70 chaperone-substrate ensemble: identified from analysis of NMR-detected titration data.
Protein Sci. 2017 Aug 19;:
Authors: Sekhar A, Nagesh J, Rosenzweig R, Kay LE
Abstract
The Hsp70 chaperone system plays a critical role in cellular homeostasis by binding to client protein molecules. We have recently shown by methyl-TROSY NMR methods that...
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08-25-2017 04:11 AM
Specific Binding of Tetratricopeptide Repeat Proteinsto Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90)Is Regulated by Affinity and Phosphorylation
Specific Binding of Tetratricopeptide Repeat Proteinsto Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90)Is Regulated by Affinity and Phosphorylation
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b00801/20151125/images/medium/bi-2015-00801d_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b00801
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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11-26-2015 12:22 PM
[NMR paper] Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Related Articles Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Biochemistry. 2004 Nov 2;43(43):13775-86
Authors: Bann JG, Frieden C
The folding of the two-domain bacterial chaperone PapD has been studied to develop an understanding of the relationship between individual domain folding and the formation of domain-domain interactions. PapD contains six phenylalanine residues, four in the N-terminal domain and two in the...
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11-24-2010 10:03 PM
[NMR paper] Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with w
Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.
Related Articles Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.
Biochemistry. 2003 Sep 30;42(38):11100-8
Authors: Cai S, Stevens SY, Budor AP, Zuiderweg ER
The interaction of solvent of the substrate binding domain of the bacterial heat shock 70 chaperone protein DnaK was studied in its apo form and with bound hydrophobic substrate peptide, using refined nuclear magnetic...