Solvent Interaction of a Hsp70 Chaperone Substrate-Binding Domain Investigated with Water−NOE NMR Experiments-Reference-Cited by-同舟云学术

Solvent Interaction of a Hsp70 Chaperone Substrate-Binding Domain Investigated with Water−NOE NMR Experiments

Published:2003-09-01 Issue:38 Volume:42 Page:11100-11108
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Cai Sheng¹,Stevens Shawn Y.¹,Budor Andrew P.¹,Zuiderweg Erik R. P.¹

Affiliation:

1. Biophysics Research Division and Departments of Biological Chemistry and Chemistry, The University of Michigan, 930 North University Avenue, Ann Arbor, Michigan 48109

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi030097c

Reference51 articles.

1. Crystal Structure of Ser-22/Ile-25 Form Crambin Confirms Solvent, Side Chain Substate Correlations

2. Calculation of Hydrodynamic Properties of Globular Proteins from Their Atomic-Level Structure

3. Heat shock proteins: molecular chaperones of protein biogenesis

4. Chaperone-assisted protein folding

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