Site-resolved measurement of water-protein interactions by solution NMR

Nathaniel V. Nucci, Maxim S. Pometun, A. Joshua Wand

Research output: Contribution to journalArticlepeer-review

174 Scopus citations

Abstract

The interactions of biological macromolecules with water are fundamental to their structure, dynamics and function. Historically, characterization of the location and residence times of hydration waters of proteins in solution has been quite difficult. Confining proteins within the nanoscale interior of a reverse micelle slows water dynamics, allowing global protein-water interactions to be detected using nuclear magnetic resonance techniques. Complications that normally arise from hydrogen exchange and long-range dipolar coupling are overcome by the nature of the reverse micelle medium. Characterization of the hydration of ubiquitin demonstrates that encapsulation within a reverse micelle allows detection of dozens of hydration waters. Comparison of nuclear Overhauser effects obtained in the laboratory and rotating frames indicate a considerable range of hydration water dynamics is present on the protein surface. In addition, an unprecedented clustering of different hydration-dynamics classes of sites is evident.

Original languageEnglish (US)
Pages (from-to)245-250
Number of pages6
JournalNature Structural and Molecular Biology
Volume18
Issue number2
DOIs
StatePublished - Feb 2011
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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