NMR Studies of Unfolded States of an SH3 Domain in Aqueous Solution and Denaturing Conditions-Reference-Cited by-同舟云学术

NMR Studies of Unfolded States of an SH3 Domain in Aqueous Solution and Denaturing Conditions

Published:1997-04-01 Issue:13 Volume:36 Page:3959-3970
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Zhang Ouwen¹,Forman-Kay Julie D.¹

Affiliation:

1. Biochemistry Research Division, Hospital for Sick Children, 555 University Avenue, Toronto, Ontario, Canada M5G 1X8, Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada M5S 1A8, and Department of Chemistry, University of Toronto, Toronto, Ontario, Canada M5S 3H6

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9627626

Reference80 articles.

1. Characterization of a Trifluoroethanol-induced Partially Folded State of α-Lactalbumin

2. A Comparison of the pH, Urea, and Temperature-denatured States of Barnase by Heteronuclear NMR: Implications for the Initiation of Protein Folding

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