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Zhou Biophysics Group at FSU

The Zhou group carries out theoretical, computational, and experimental studies on the structure, dynamics, and function of proteins. Four main directions are: (1) allostery and binding kinetics of structured and disordered proteins; (2) crowding and emergent properties in cellular environments; (3) structure and function of ion channels and other membrane proteins; and (4) structures and mechanisms of peptide self-assembly.


C. Guo and H.-X. Zhou (2016). Unidirectional allostery in the regulatory subunit RI╬▒ facilitates efficient deactivation of protein kinase A. 113, E6776-E6785.pdf

S. Qin and H.-X. Zhou (2016). Fast method for computing chemical potentials and liquid-liquid phase equilibria of macromolecular solutions. J. Phys. Chem. B. 120,8164-8174.pdf

J. Dai and H.-X. Zhou (2016). Semiclosed conformations of the ligand-binding domains of NMDA receptors during stationary gating. Biophys. J. 111, 1418-1428..pdf

A. R. Cormier, X. Pang, M. I. Zimmerman, H.-X. Zhou, and A. K. Paravastu (2013). Molecular structure of RADA16-I designer self-assembling peptide nanofibers. ACS Nano 7, 7562-7572.pdf

  • Laboratory and Office
  •       Room 419/419A (Computational) and Room 322/407 (Experimental)
          Kasha Laboratory of Biophysics, Florida State University
          Tallahassee, FL 32306
          Phone: (850) 645-1336(office)/1334(lab); Fax: (850) 644-7244