Ligand-dependent folding and unfolding dynamics and free energy landscapes of acylphosphatase-Reference-Cited by-同舟云学术

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Ligand-dependent folding and unfolding dynamics and free energy landscapes of acylphosphatase

Published:2024 Issue:18 Volume:20 Page:3780-3786
ISSN:1744-683X
Container-title:Soft Matter
language:en
Short-container-title:Soft Matter

Author:

Yuan Li¹,Sun Hao²^ORCID,Ma Xuening¹,Wang Yang²,Guo Zilong²,Qi Xingyu¹²,Le Shimin¹,Chen Hu¹²^ORCID

Affiliation:

1. Research Institute for Biomimetics and Soft Matter, Fujian Provincial Key Lab for Soft Functional Materials Research, Department of Physics, Xiamen University, Xiamen 361005, China

2. Center of Biomedical Physics, Wenzhou Institute, University of Chinese Academy of Sciences, Wenzhou 325000, China

Abstract

The free energy landscapes of AcP in the absence and presence of Pi are constructed by using stable magnetic tweezers.

Funder

National Natural Science Foundation of China

Higher Education Discipline Innovation Project

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/SM/D4SM00131A

Reference33 articles.

1. Thermodynamics of Protein–Ligand Interactions: History, Presence, and Future Aspects

2. Insights into Protein–Ligand Interactions: Mechanisms, Models, and Methods

3. The Protein-Folding Problem, 50 Years On

4. Protein folding and misfolding

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