Transmembrane protein activation refined by site-specific hydration dynamics

Sunyia Hussain; John M. Franck; Songi Han

doi:10.1002/anie.201206147

Transmembrane protein activation refined by site-specific hydration dynamics

Sunyia Hussain, John M. Franck, Songi Han

Research output: Contribution to journal › Article › peer-review

46 Scopus citations

Abstract

Proteins on film: The Overhauser dynamic nuclear polarization method resolves hydration dynamics to an unprecedented level of detail for a transmembrane protein surface. The heterogeneous hydration landscape of proteorhodopsin rearranges upon photoactivation (see picture), thus providing an insight into how water contributes to protein function even for biological systems embedded in a hydrophobic membrane.

Original language	English (US)
Pages (from-to)	1953-1958
Number of pages	6
Journal	Angewandte Chemie - International Edition
Volume	52
Issue number	7
DOIs	https://doi.org/10.1002/anie.201206147
State	Published - Feb 11 2013
Externally published	Yes

Keywords

EPR spectroscopy
dynamic nuclear polarization
hydration dynamics
membrane proteins
proteorhodopsin

ASJC Scopus subject areas

Catalysis
General Chemistry

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10.1002/anie.201206147

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abstract = "Proteins on film: The Overhauser dynamic nuclear polarization method resolves hydration dynamics to an unprecedented level of detail for a transmembrane protein surface. The heterogeneous hydration landscape of proteorhodopsin rearranges upon photoactivation (see picture), thus providing an insight into how water contributes to protein function even for biological systems embedded in a hydrophobic membrane.",

keywords = "EPR spectroscopy, dynamic nuclear polarization, hydration dynamics, membrane proteins, proteorhodopsin",

author = "Sunyia Hussain and Franck, {John M.} and Songi Han",

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AU - Franck, John M.

AU - Han, Songi

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AB - Proteins on film: The Overhauser dynamic nuclear polarization method resolves hydration dynamics to an unprecedented level of detail for a transmembrane protein surface. The heterogeneous hydration landscape of proteorhodopsin rearranges upon photoactivation (see picture), thus providing an insight into how water contributes to protein function even for biological systems embedded in a hydrophobic membrane.

KW - EPR spectroscopy

KW - dynamic nuclear polarization

KW - hydration dynamics

KW - membrane proteins

KW - proteorhodopsin

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Transmembrane protein activation refined by site-specific hydration dynamics

Abstract

Keywords

ASJC Scopus subject areas

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