Distinct Protein Hydration Water Species Defined by Spatially Resolved Spectra of Intermolecular Vibrations

Viren Pattni, Tatiana Vasilevskaya, Walter Thiel, Matthias Heyden

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


In this molecular dynamics simulation study, we analyze intermolecular vibrations in the hydration shell of a solvated enyzme, the membrane type 1-matrix metalloproteinase, with high spatial resolution. Our approach allows us to characterize vibrational signatures of the local hydrogen bond network, the translational mobility of water molecules, as well as the molecular entropy, in specific local environments. Our study demonstrates the heterogeneity of water properties within the hydration shell of a complex biomolecule. We define a classification scheme based on the vibrational density of states that allows us to distinguish separate classes of hydration water species and facilitates the description of hydration water properties at distinct hydration sites. The results demonstrate that no single characteristic of the protein surface is sufficient to determine the properties of nearby water. The protein surface geometry, quantified here by the number of protein atoms in the vicinity of a hydration water molecule, as well as the chemical nature of a solvated protein functional group, influences dynamic and thermodynamic properties of solvating water molecules.

Original languageEnglish (US)
Pages (from-to)7431-7442
Number of pages12
JournalJournal of Physical Chemistry B
Issue number31
StatePublished - Aug 10 2017
Externally publishedYes

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry


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