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two-state model explaining thermodynamic regulation of thermogating channels

Biophysics Reports 2022年第4期8卷 205-211页

作者： Xuejun C.Zhang Zhuoya Yu National Laboratory of Biomacromolecules CAS Center for Excellence in Biomacromolecules Institute of Biophysics Chinese Academy of Sciences College of Life Sciences University of Chinese Academy of Sciences

Temperature-sensitive ion channels, such as those from the TRP family(thermo-TRPs) present in all animal cells, serve to perceive heat and cold sensations. A considerable number of protein structures have been reported for these ion channels, providing a solid basis for revealing their structure–function relationship. Previous functional studies suggest that the thermosensing ability of TRP channels is primarily determined by the properties of their cytosolic domain. Despite their importance in sensing and wide interests in the development of suitable therapeutics, the precise mechanisms underlying acute and steep temperature-mediated channel gating remain enigmatic. Here, we propose a model in which the thermo-TRP channels directly sense external temperature through the formation and dissociation of metastable cytoplasmic domains. An open–close bistable system is described in the framework of equilibrium thermodynamics, and the middle-point temperature T? similar to the V?parameter for a voltage-gating channel is defined. Based on the relationship between channel opening probability and temperature, we estimate the change in entropy and enthalpy during the conformational change for a typical thermosensitive channel. Our model is able to accurately reproduce the steep activation phase in experimentally determined thermal-channel opening curves, and thus should greatly facilitate future experimental verification.

关键词： Temperature sensing Thermo-TRPs Thermo-gating channel two-state model Differential conformation energy

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Folding nucleus and unfolding dynamics of protein 2GB1

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Chinese Physics B 2021年第2期30卷 116-120页

作者： Xuefeng Wei Yanting Wang CAS Key Laboratory of Theoretical Physics Institute of Theoretical PhysicsChinese Academy of SciencesBeijing 100190China School of Physical Sciences University of Chinese Academy of SciencesBeijing 100049China

The folding of many small proteins is kinetically a two-state process with one major free-energy barrier to overcome,which can be roughly regarded as the inverse process of *** this work,we first use a Gaussian network model to predict the folding nucleus corresponding to the major free-energy barrier of protein 2 GB1,and find that the folding nucleus is located in theβ-sheet ***-temperature molecular dynamics simulations are then used to investigate the unfolding process of 2 *** draw free-energy surface from unfolding simulations,taking RMSD and contact number as reaction coordinates,which confirms that the folding of 2 GB1 is kinetically a two-state *** comparison of the contact maps before and after the free energy barrier indicates that the transition from native to non-native structure of the protein is kinetically caused by the destruction of theβ-sheet domain,which manifests that the folding nucleus is indeed located in theβ-sheet ***,the constrained MD simulation further confirms that the destruction of the secondary structures does not alter the topology of the protein retained by the folding *** results provide vital information for upcoming researchers to further understand protein folding in similar systems.

关键词： protein folding 2GB1 two-state model folding nucleus

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