H
Huan-Xiang Zhou
Researcher at University of Illinois at Chicago
Publications - 332
Citations - 19612
Huan-Xiang Zhou is an academic researcher from University of Illinois at Chicago. The author has contributed to research in topics: Macromolecular crowding & Protein structure. The author has an hindex of 70, co-authored 316 publications receiving 17825 citations. Previous affiliations of Huan-Xiang Zhou include Florida State University & Drexel University.
Papers
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Macromolecular Crowding and Confinement: Biochemical, Biophysical, and Potential Physiological Consequences*
TL;DR: Theoretical and experimental approaches to the characterization of crowding- and confinement-induced effects in systems approaching the complexity of living organisms are suggested.
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Calculation of protein-ligand binding affinities.
TL;DR: This paper reviews physics-based models of binding, beginning with a summary of the changes in potential energy, solvation energy, and configurational entropy that influence affinity, and a theoretical overview to frame the discussion of specific computational approaches.
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Fundamental aspects of protein-protein association kinetics.
TL;DR: This review focuses on recent advances in deciphering the kinetic pathway of protein complex formation, the nature of the pre-complex formed through diffusion, the transition state, and other intermediates (such as the so-called encounter complex) along the association pathway.
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Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation
Huan-Xiang Zhou,Xiaodong Pang +1 more
TL;DR: This review will examine how charged side chains are spatially distributed in various types of proteins and how electrostatic interactions affect thermodynamic and kinetic properties of proteins.
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Insight into the Mechanism of the Influenza A Proton Channel from a Structure in a Lipid Bilayer
Mukesh Sharma,Myunggi Yi,Hao Dong,Huajun Qin,Emily B. Peterson,David D. Busath,Huan-Xiang Zhou,Timothy A. Cross +7 more
TL;DR: The structure of the M2 conductance domain in a lipid bilayer is determined and it is proposed that the tetrameric His37-Trp41 cluster guides protons through the channel by forming and breaking hydrogen bonds between adjacent pairs of histidines and through specific interactions of the histidine with the tryptophan gate.