Allosteric Type and Pathways Are Governed by the Forces of Protein–Ligand Binding-Reference-Cited by-同舟云学术

Allosteric Type and Pathways Are Governed by the Forces of Protein–Ligand Binding

Published:2021-06-03 Issue:22 Volume:12 Page:5404-5412
ISSN:1948-7185
Container-title:The Journal of Physical Chemistry Letters
language:en
Short-container-title:J. Phys. Chem. Lett.

Author:

Huang Qiaojing¹,Song Pengbo¹,Chen Yixin¹,Liu Zhirong¹^ORCID,Lai Luhua¹²³^ORCID

Affiliation:

1. Beijing National Laboratory for Molecular Sciences (BNLMS), State Key Laboratory for Structural Chemistry of Unstable and Stable Species, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China

2. Center for Quantitative Biology, Peking University, Beijing 100871, China

3. Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, 100871, China

Funder

National Natural Science Foundation of China

National Science and Technology Major Project

Publisher

American Chemical Society (ACS)

Subject

General Materials Science,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpclett.1c01253

Reference63 articles.

1. General Conclusions: Teleonomic Mechanisms in Cellular Metabolism, Growth, and Differentiation

2. On the nature of allosteric transitions: A plausible model

3. Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*

4. The determination of thermodynamic allosteric parameters of an enzyme undergoing steady-state turnover

5. The ensemble nature of allostery

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