Slow Dynamics in Folded and Unfolded States of an SH3 Domain-Reference-Cited by-同舟云学术

Slow Dynamics in Folded and Unfolded States of an SH3 Domain

Published:2001-10-26 Issue:46 Volume:123 Page:11341-11352
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Tollinger Martin¹,Skrynnikov Nikolai R.¹,Mulder Frans A. A.¹,Forman-Kay Julie D.¹,Kay Lewis E.¹

Affiliation:

1. Contributions from the Structural Biology and Biochemistry Program, Hospital for Sick Children, Toronto, Ontario, Canada M5G 1X8, Protein Engineering Network Center of Excellence and Departments of Medical Genetics and Chemistry, University of Toronto, Toronto, Ontario, Canada M5S 1A8, and Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada M5S 1A8

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja011300z

Reference49 articles.

1. Equilibrium NMR studies of unfolded and partially folded proteins

2. Probing molecular motion by NMR

3. New techniques in structural NMR — anisotropic interactions

4. Comparison of the Backbone Dynamics of a Folded and an Unfolded SH3 Domain Existing in Equilibrium in Aqueous Buffer

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