Ruhong Zhou

Affiliations: 
2000- IBM Thomas J. Watson Research Center, Yorktown Heights, NY, United States 
Area:
novel algorithms for computational biology and bioinformatics, protein folding dynamics, protein-protein interaction, and ligand-receptor binding mechanism
Website:
http://www.columbia.edu/cu/chemistry/adjunct-faculty-bios/zhou/adjunct.html
Google:
"Ruhong Zhou"
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Parents

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Bruce J. Berne grad student 1997 Columbia
 (Novel methods for efficient sampling of conformation space of proteins)
Richard A. Friesner post-doc Columbia
William L. Jorgensen post-doc Yale
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Publications

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Weber JK, Kang SG, Zhou R. (2018) Rare Dissipative Transitions Punctuate the Initiation of Chemical Denaturation in Proteins. Biophysical Journal. 114: 812-821
Zhang L, Feng M, Zhou R, et al. (2017) Structural Perturbations on Huntingtin N17 Domain during its Folding on 2D-Nanomaterials. Nanotechnology
Gu Z, De Luna P, Yang Z, et al. (2017) Structural influence of proteins upon adsorption to MoS2 nanomaterials: comparison of MoS2 force field parameters. Physical Chemistry Chemical Physics : Pccp
Gu Z, Yang Z, Kang SG, et al. (2016) Robust Denaturation of Villin Headpiece by MoS2 Nanosheet: Potential Molecular Origin of the Nanotoxicity. Scientific Reports. 6: 28252
Xu Z, Zhang S, Weber JK, et al. (2016) Sequential protein unfolding through a carbon nanotube pore. Nanoscale
Luan B, Huynh T, Zhou R. (2016) Potential Interference of Protein-Protein Interactions by Graphyne. The Journal of Physical Chemistry. B
Luan B, Huynh T, Li J, et al. (2015) Nanomechanics of Protein Unfolding Outside a Generic Nanopore. Acs Nano
Gu Z, Yang Z, Wang L, et al. (2015) The role of basic residues in the adsorption of blood proteins onto the graphene surface. Scientific Reports. 5: 10873
Stirnemann G, Kang SG, Zhou R, et al. (2014) How force unfolding differs from chemical denaturation. Proceedings of the National Academy of Sciences of the United States of America. 111: 3413-8
Xia Z, Das P, Shakhnovich EI, et al. (2012) Collapse of unfolded proteins in a mixture of denaturants. Journal of the American Chemical Society. 134: 18266-74
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