Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 40, Pages 17101-17106Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1011569107
Keywords
fluorine; noncanonical amino acids; protein engineering; solvation dynamics; ultrafast hydration
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Funding
- National Institutes of Health (NIH) [GM62523]
- National Science Foundation (NSF) [DMR-0964886]
- Office of Naval Research (ONR) [N00014-03-1-0793]
- Samsung
- National Defense Science and Engineering Graduate Fellowship
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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.
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