Huanjie Jiang, Yanwei Wang, Jiayuan Chen, Dan Hu, Hai Pan, Zilong Guo, Hu Chen
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Mutation in a Non-Force-Bearing Region of Protein L Influences Force-Dependent Unfolding Behavior
Single-molecule magnetic tweezers (MT) have revealed multiple transition barriers along the unfolding pathway of several two-state proteins, such as GB1 and Csp. In this study, we utilized MT to measure the force-dependent folding and unfolding rates of both the 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 to 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 PLWT. Our finding demonstrates that the residue outside of the force-bearing region will also affect the force-induced unfolding dynamics.
期刊介绍:
Chinese Physics B is an international journal covering the latest developments and achievements in all branches of physics worldwide (with the exception of nuclear physics and physics of elementary particles and fields, which is covered by Chinese Physics C). It publishes original research papers and rapid communications reflecting creative and innovative achievements across the field of physics, as well as review articles covering important accomplishments in the frontiers of physics.
Subject coverage includes:
Condensed matter physics and the physics of materials
Atomic, molecular and optical physics
Statistical, nonlinear and soft matter physics
Plasma physics
Interdisciplinary physics.