Water rotation barriers on protein molecular surfaces

K. Tompa, M. Bokor, T. Verebélyi, P. Tompa

Research output: Contribution to journalArticle

15 Citations (Scopus)


The experimental characterization of hindered-rotation barriers and mapping the energetic heterogeneity of water molecules bound to the molecular "surface" of proteins is critical for understanding the functional interaction of proteins with their environment. Here, we show how to achieve this goal by an original wide-line NMR procedure, which is based on the spectral motional narrowing phenomenon following the melting (thawing) process of interfacial ice. The procedure highlights the differences between globular and intrinsically disordered proteins and it enables to delineate the effect of solvent on protein structure, making a distinction between point mutants, monomeric and oligomeric states, and characterizing the molecular interactions taking part in different cellular processes. We put this unique experimental approach introducing novel physical quantities and quantifying the heterogeneous distribution of motional activation energy of water in the interfacial landscape into a historical perspective, demonstrating its utility through a variety of globular and disordered proteins.

Original languageEnglish
Pages (from-to)15-25
Number of pages11
JournalChemical Physics
Publication statusPublished - Feb 20 2015


  • Interfacial water
  • NMR
  • Order parameter
  • Protein hydration
  • Proteins
  • Rotation barriers
  • Wide-line

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

Fingerprint Dive into the research topics of 'Water rotation barriers on protein molecular surfaces'. Together they form a unique fingerprint.

  • Cite this