Reverse micelles as a tool for probing solvent modulation of protein dynamics: Reverse micelle encapsulated hemoglobin

Camille J. Roche, David Dantsker, Elizabeth R. Heller, Joseph E. Sabat, Joel M. Friedman

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

Hydration waters impact protein dynamics. Dissecting the interplay between hydration waters and dynamics requires a protein that manifests a broad range of dynamics. Proteins in reverse micelles (RMs) have promise as tools to achieve this objective because the water content can be manipulated. Hemoglobin is an appropriate tool with which to probe hydration effects. We describe both a protocol for hemoglobin encapsulation in reverse micelles and a facile method using PEG and cosolvents to manipulate water content. Hydration properties are probed using the water-sensitive fluorescence from Hb bound pyranine and covalently attached Badan. Protein dynamics are probed through ligand recombination traces derived from photodissociated carbonmonoxy hemoglobin on a log scale that exposes the potential role of both a and p solvent fluctuations in modulating protein dynamics. The results open the possibility of probing hydration level phenomena in this system using a combination of NMR and optical probes.

Original languageEnglish (US)
Pages (from-to)88-97
Number of pages10
JournalChemical Physics
Volume422
DOIs
StatePublished - Jan 1 2013

Keywords

  • Geminate recombination
  • Hemoglobin
  • Hydration
  • Protein dynamics
  • Reverse micelles
  • Solvent slaving

ASJC Scopus subject areas

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

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