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Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
DnaK is the canonical Hsp70 molecular chaperone protein from Escherichia coli. Like other Hsp70s, DnaK comprises two main domains: a 44-kDa N-terminal nucleotide-binding domain (NBD) that containsExpand
Mapping protein-protein interactions in solution by NMR spectroscopy.
NMR is very well suited to the study of especially weak protein-protein interactions, as no crystallization is required. The available NMR methods to this end are reviewed and illustrated withExpand
Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface
The heat shock protein 70 kDa (Hsp70)/DnaJ/nucleotide exchange factor system assists in intracellular protein (re)folding. Using solution NMR, we obtained a three-dimensional structure for a 75-kDaExpand
High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70.
The three-dimensional structure for the substrate-binding domain of the mammalian chaperone protein Hsc70 of the 70 kDa heat shock class (HSP70) is presented. This domain includes residues 383-540Expand
Structural insights into substrate binding by the molecular chaperone DnaK
How substrate affinity is modulated by nucleotide binding remains a fundamental, unanswered question in the study of 70 kDa heat shock protein (Hsp70) molecular chaperones. We find here that theExpand
Allosteric drugs: the interaction of antitumor compound MKT-077 with human Hsp70 chaperones.
Hsp70 (heat shock protein 70 kDa) chaperones are key to cellular protein homeostasis. However, they also have the ability to inhibit tumor apoptosis and contribute to aberrant accumulation ofExpand
Allostery in the Hsp70 chaperone proteins.
Heat shock 70-kDa (Hsp70) chaperones are essential to in vivo protein folding, protein transport, and protein re-folding. They carry out these activities using repeated cycles of binding and releaseExpand
Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40.
Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in protein homeostasis. In these various tasks, the activity of Hsp70 is shaped by interactions withExpand
The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393–507) in complex with the peptide NRLLLTG
The Hsp70 family of molecular chaperones participates in a number of cellular processes, including binding to nascent polypeptide chains and assistance in protein (re)folding and degradation. WeExpand
Heteronuclear three-dimensional nmr spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra
Recently, three-dimensional Fourier transform techniques have been suggested (I3) as a possible method to resolve the spectra of complicated systems. Analogous to the comparison of 2D with 1 D NMR,Expand
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