中国物理B(英文版)2024,Vol.33Issue(7) :623-629.DOI:10.1088/1674-1056/ad3dcd

Mutation in a non-force-bearing region of protein L influences force-dependent unfolding behavior

蒋环杰 王艳伟 陈家媛 胡丹 潘海 郭子龙 陈虎
中国物理B(英文版)2024,Vol.33Issue(7) :623-629.DOI:10.1088/1674-1056/ad3dcd

Mutation in a non-force-bearing region of protein L influences force-dependent unfolding behavior

蒋环杰 1王艳伟 2陈家媛 1胡丹 1潘海 3郭子龙 3陈虎4
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作者信息

  • 1. Department of Physics,Wenzhou University,Wenzhou 325035,China;Center of Biomedical Physics,Wenzhou Institute,University of Chinese Academy of Sciences,Wenzhou 325000,China
  • 2. Department of Physics,Wenzhou University,Wenzhou 325035,China
  • 3. Center of Biomedical Physics,Wenzhou Institute,University of Chinese Academy of Sciences,Wenzhou 325000,China
  • 4. Center of Biomedical Physics,Wenzhou Institute,University of Chinese Academy of Sciences,Wenzhou 325000,China;Research Institute for Biomimetics and Soft Matter,Fujian Provincial Key Laboratory for Soft Functional Materials Research,Department of Physics,Xiamen University,Xiamen 361005,China
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Abstract

Single-molecule magnetic tweezers(MTs)have revealed multiple transition barriers along the unfolding pathway of several two-state proteins,such as GB1 and Csp.In this study,we utilized MTs to measure the force-dependent folding and unfolding rates of both protein L(PLWT)and its Y47W mutant(PLY47W)where the mutation point is not at the force-bearing β-strands.The measurements were conducted within a force range of 3-120 pN.Notably,the unfolding rates of both PLWT and PWY47W exhibit distinct force sensitivities below 50 pN and above 60 pN,implying a two-barrier free energy landscape.Both PLWT and PLY47W share the same force-dependent folding rate and the same transition barriers,but the unfolding rate of PLY47W is faster than that of PLWT.Our finding demonstrates that the residue outside of the force-bearing region will also affect the force-induced unfolding dynamics.

Key words

protein folding/magnetic tweezers/protein L

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基金项目

National Natural Science Foundation of China(12174322)

National Natural Science Foundation of China(12204124)

111 Project(B16029)

Graduate Scientific Research Foundation of Wenzhou University(3162023003034)

research grant from Wenzhou Institute()

出版年

2024
中国物理B(英文版)
中国物理学会和中国科学院物理研究所

中国物理B(英文版)

CSTPCDEI
影响因子:0.995
ISSN:1674-1056
参考文献量28
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