Protein-water interface

The interface between a protein and hydration water is heterogeneous both dynamically and statistically. The structure of interface affects the electrostatics at protein's active site and rates of chemical reactions carried by enzymes. In our current projects we address the following questions: (i) Does the interfacial ``biological'' water produce electrostatic signatures specific to proteins? (ii) What is the spectrum of interfacial electrostatic fluctuations? (iii) How is protein-mediated chemistry affected by electrostatics?  


  • "Dipolar nanodomains in protein hydration shells", D. R. Martin and D. V. Matyushov, J. Phys. Chem. Lett. 6, 407 (2015)
  • "Hydration shells of proteins probed by depolarized light scattering and dielectric spectroscopy: Orientational structure is significant, positional structure is not", J. Chem. Phys. 141, 22D501 (2014)
  • "Solvated dissipative electro-elastic network model of hydrated proteins", D. R. Martin and D. V. Matyushov, J. Chem. Phys. 137, 165101 (2012)
  • "Electrostatics of the protein-water interface and the dynamical transition in proteins", D. V. Matyushov and A. Y. Morozov, Phys. Rev. E 84, 011908 (2011)

Ordering of water in dipolar domains at the surface of lysozyme

Nanodomains in the hydration shell of lysozyme extend 12−15 Å from the protein surface into the bulk. They are characterized by orientational order parameters of water in the interface. The formation of nano-domains is also reflected by the dipolar susceptibility of the hydration shells with phenomenology similar to that of relaxor ferroelectrics.