首页|Mutation in a non-force-bearing region of protein L influences force-dependent unfolding behavior
Mutation in a non-force-bearing region of protein L influences force-dependent unfolding behavior
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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.
protein foldingmagnetic tweezersprotein L
蒋环杰、王艳伟、陈家媛、胡丹、潘海、郭子龙、陈虎
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Department of Physics,Wenzhou University,Wenzhou 325035,China
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
National Natural Science Foundation of ChinaNational Natural Science Foundation of China111 ProjectGraduate Scientific Research Foundation of Wenzhou Universityresearch grant from Wenzhou Institute
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