Single-molecule scale quantification reveals interactions underlying protein–protein interface: from forces to non-covalent bonds-Reference-Cited by-同舟云学术

Single-molecule scale quantification reveals interactions underlying protein–protein interface: from forces to non-covalent bonds

Published:2023 Issue:46 Volume:25 Page:31791-31803
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Sun Heng¹,Tian Yichen¹,Fu Yuna¹,Lei Yongrong¹,Wang Yani¹,Yan Xinrui¹,Wang Jianhua¹^ORCID

Affiliation:

1. Key Laboratory of Biorheological Science and Technology, Ministry of Education, College of Bioengineering, Chongqing University, Chongqing, 400044, China

Abstract

Using atomic force microscopy-based single-molecule force spectroscopy to quantify noncovalent binding between BAX and Bcl-2, and observing that complicated multivalent binding interactions induced stable BAX/Bcl-2 complexes.

Funder

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CP/D3CP04351G

Reference65 articles.

1. Antiapoptotic potency of Bcl-2 proteins primarily relies on their stability, not binding selectivity

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4. BAK/BAX activation and cytochrome c release assays using isolated mitochondria

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