Domain Swapping Proceeds via Complete Unfolding: A 19F- and 1H-NMR Study of the Cyanovirin-N Protein-Reference-Cited by-同舟云学术

Domain Swapping Proceeds via Complete Unfolding: A 19F- and 1H-NMR Study of the Cyanovirin-N Protein

Published:2012-02-22 Issue:9 Volume:134 Page:4229-4235
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Liu Lin¹²,Byeon In-Ja L.¹,Bahar Ivet²,Gronenborn Angela M.¹

Affiliation:

1. Department of Structural Biology, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, Pennsylvania 15261, United States

2. Department of Computational and Systems Biology, University of Pittsburgh School of Medicine, 3076 Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, Pennsylvania 15261, United States

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja210118w

Reference42 articles.

1. The Energy Landscapes and Motions of Proteins

2. 3D domain swapping: A mechanism for oligomer assembly

3. The Protein Data Bank

4. The antitumor action of seminal ribonuclease and its quaternary conformations

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