What is he best known for?
The fields of study he is best known for:
- Enzyme
- Quantum mechanics
- Gene
His primary scientific interests are in Crystallography, Protein structure, Biophysics, Plasma protein binding and Protein folding.
Huan-Xiang Zhou has included themes like Barnase, M2 proton channel, Barstar, Nuclear magnetic resonance spectroscopy and Molecule in his Crystallography study.
His studies in Protein structure integrate themes in fields like Docking, Macromolecule, Binding site, Hydrogen bond and Self-assembling peptide.
His Biophysics study combines topics in areas such as NMDA receptor, Glutamate receptor, Biochemistry, Excitatory Amino Acid Agonist and Crowding.
His biological study spans a wide range of topics, including Chemical physics, Macromolecular crowding, Data-driven, Folding and Simulation.
His Chemical physics study incorporates themes from Electrostatics and Computational chemistry.
His most cited work include:
- Macromolecular Crowding and Confinement: Biochemical, Biophysical, and Potential Physiological Consequences* (1446 citations)
- Calculation of protein-ligand binding affinities. (678 citations)
- Fundamental aspects of protein-protein association kinetics. (483 citations)
What are the main themes of his work throughout his whole career to date?
Huan-Xiang Zhou spends much of his time researching Biophysics, Crystallography, Protein structure, Molecular dynamics and Chemical physics.
He combines subjects such as Folding, Macromolecule, Macromolecular crowding, Biochemistry and Transmembrane domain with his study of Biophysics.
His Crystallography study combines topics in areas such as M2 proton channel, Protein folding, Molecule, Nuclear magnetic resonance spectroscopy and Lipid bilayer.
The various areas that Huan-Xiang Zhou examines in his Protein folding study include Crowding, Static electricity and Thermodynamics.
He focuses mostly in the field of Protein structure, narrowing it down to matters related to Plasma protein binding and, in some cases, Binding site and Docking.
His Chemical physics research includes elements of Electrostatics, Computational chemistry and Ion.
He most often published in these fields:
- Biophysics (32.29%)
- Crystallography (23.51%)
- Protein structure (18.13%)
What were the highlights of his more recent work (between 2015-2021)?
- Biophysics (32.29%)
- Macromolecule (11.05%)
- Molecular dynamics (16.71%)
In recent papers he was focusing on the following fields of study:
His primary areas of investigation include Biophysics, Macromolecule, Molecular dynamics, Intrinsically disordered proteins and Chemical physics.
His research in Biophysics intersects with topics in Plasma protein binding, Cellular functions, Phase and Membrane, Transmembrane domain.
His Plasma protein binding research integrates issues from Protein folding, Folding, Reaction rate constant, Receptor–ligand kinetics and Binding site.
In his research, Protein structure, Helix and Lipid bilayer is intimately related to Hydrogen bond, which falls under the overarching field of Molecular dynamics.
His Chemical physics research is multidisciplinary, incorporating perspectives in Electrostatics, Surface tension and Intermolecular force.
His work carried out in the field of Crystallography brings together such families of science as Docking, Interaction energy and Ligand.
Between 2015 and 2021, his most popular works were:
- Protein Allostery and Conformational Dynamics. (165 citations)
- Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation (162 citations)
- Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation (162 citations)
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