Combining THz spectroscopy and MD simulations to study protein-hydration coupling

Matthias Heyden, Martina Havenith

Research output: Contribution to journalArticlepeer-review

119 Scopus citations

Abstract

THz spectroscopy is combined with MD simulations to study the dynamical properties of water in the solvation shell of proteins. The solvation dynamics is found to be influenced on length-scales of several hydration layers which is significantly more than what is found for static properties. Our experiments show that the properties of this dynamical solvation shell depend on the folding state of the protein. Kinetic THz absorption studies allow us to observe the formation of the dynamical solvation shell of the native protein upon folding. The experimental results can be reproduced using MD simulations which helps to develop a molecular understanding in terms of retardation of water dynamics.

Original languageEnglish (US)
Pages (from-to)74-83
Number of pages10
JournalMethods
Volume52
Issue number1
DOIs
StatePublished - Sep 2010
Externally publishedYes

Keywords

  • Folding
  • Low frequency motions
  • MD simulations
  • Protein dynamics
  • Protein folding
  • Proteins
  • Solvation
  • Solvation dynamics
  • THz spectroscopy

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)

Fingerprint

Dive into the research topics of 'Combining THz spectroscopy and MD simulations to study protein-hydration coupling'. Together they form a unique fingerprint.

Cite this