Quantitative Analysis of Multisite Protein–Ligand Interactions by NMR: Binding of Intrinsically Disordered p53 Transactivation Subdomains with the TAZ2 Domain of CBP-Reference-Cited by-同舟云学术

Quantitative Analysis of Multisite Protein–Ligand Interactions by NMR: Binding of Intrinsically Disordered p53 Transactivation Subdomains with the TAZ2 Domain of CBP

Published:2012-02-15 Issue:8 Volume:134 Page:3792-3803
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Arai Munehito¹²³⁴,Ferreon Josephine C.¹,Wright Peter E.¹

Affiliation:

1. Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, United States

2. Institute for Biological Resources and Functions, AIST, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan

3. Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, 3-8-1 Komaba, Meguro, Tokyo 153-8902, Japan

4. PRESTO, JST, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja209936u

Reference54 articles.

1. NMR methods for the determination of protein–ligand dissociation constants

2. [8] Singular value decomposition: Application to analysis of experimental data