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Proc Natl Acad Sci U S A. 2010 Oct 5;107(40):17101-6. doi: 10.1073/pnas.1011569107. Epub 2010 Sep 20.

Hydration dynamics at fluorinated protein surfaces.

Author information

1
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.

Abstract

Water-protein interactions dictate many processes crucial to protein function including folding, dynamics, interactions with other biomolecules, and enzymatic catalysis. Here we examine the effect of surface fluorination on water-protein interactions. Modification of designed coiled-coil proteins by incorporation of 5,5,5-trifluoroleucine or (4S)-2-amino-4-methylhexanoic acid enables systematic examination of the effects of side-chain volume and fluorination on solvation dynamics. Using ultrafast fluorescence spectroscopy, we find that fluorinated side chains exert electrostatic drag on neighboring water molecules, slowing water motion at the protein surface.

PMID:
20855583
PMCID:
PMC2951393
DOI:
10.1073/pnas.1011569107
[Indexed for MEDLINE]
Free PMC Article
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