Probing Residual Interactions in Unfolded Protein States Using NMR Spin Relaxation Techniques: An Application to Δ131Δ-Reference-Cited by-同舟云学术

Probing Residual Interactions in Unfolded Protein States Using NMR Spin Relaxation Techniques: An Application to Δ131Δ

Published:2003-09-06 Issue:39 Volume:125 Page:11988-11992
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Choy Wing-Yiu¹,Kay Lewis E.¹

Affiliation:

1. Contribution from the Protein Engineering Network Centers of Excellence and Departments of Medical Genetics and Microbiology, Biochemistry, and Chemistry, 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/ja035705q

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4. Protein folding for realists: A timeless phenomenon

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