Mosaic Cooperativity in Slow Polypeptide Topological Isomerization Revealed by Residue-Specific NMR Thermodynamic Analysis-Reference-Cited by-同舟云学术

Mosaic Cooperativity in Slow Polypeptide Topological Isomerization Revealed by Residue-Specific NMR Thermodynamic Analysis

Published:2020-02-18 Issue:5 Volume:11 Page:1934-1939
ISSN:1948-7185
Container-title:The Journal of Physical Chemistry Letters
language:en
Short-container-title:J. Phys. Chem. Lett.

Author:

Fujinami Daisuke¹,Motomura Hajime¹,Oshima Hiraku²,Mahin Abdullah-Al³^ORCID,Elsayed Khaled M.³,Zendo Takeshi³,Sugita Yuji²⁴⁵^ORCID,Sonomoto Kenji³,Kohda Daisuke¹^ORCID

Affiliation:

1. Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan

2. Laboratory for Biomolecular Function Simulation, RIKEN Center for Biosystems Dynamics Research, Kobe 650-0047, Japan

3. Laboratory of Microbial Technology, Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University, Fukuoka 819-0395, Japan

4. Theoretical Molecular Science Laboratory, RIKEN Cluster for Pioneering Research, Saitama 351-0198, Japan

5. Computational Biophysics Research Team, RIKEN Center for Computational Science, Kobe 650-0047, Japan

Funder

Ministry of Education, Culture, Sports, Science and Technology

Publisher

American Chemical Society (ACS)

Subject

General Materials Science,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpclett.9b03591

Reference30 articles.

1. The present view of the mechanism of protein folding