1H−13C Dipole−Dipole Cross-Correlated Spin Relaxation As a Probe of Dynamics in Unfolded Proteins: Application to the DrkN SH3 Domain-Reference-Cited by-同舟云学术

1H−13C Dipole−Dipole Cross-Correlated Spin Relaxation As a Probe of Dynamics in Unfolded Proteins: Application to the DrkN SH3 Domain

Published:1999-03-27 Issue:14 Volume:121 Page:3555-3556
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Yang Daiwen¹,Mok Yu-Keung¹,Muhandiram D. R.¹,Forman-Kay Julie D.¹,Kay Lewis E.¹

Affiliation:

1. Protein Engineering Network Centers of Excellence and the Departments of Medical Genetics Biochemistry and Chemistry University of Toronto, Toronto, Ontario, Canada M5S 1A8 Structural Biology and Biochemistry Program Hospital for Sick Children Toronto, Ontario, Canada, M5G 1X8 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/ja9900914

Reference23 articles.

1. Structural analysis of non-native states of proteins by NMR methods

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

3. Characterization of the Backbone Dynamics of Folded and Denatured States of an SH3 Domain

4. Backbone Dynamics of a Highly Disordered 131 Residue Fragment of Staphylococcal Nuclease

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