Hydration dynamics at fluorinated protein surfaces
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- Hydration dynamics at fluorinated protein surfaces
- Kwon, Oh Hoon; Yoo, Tae Hyeon; Othona, Christina M.; Van Deventer, James A.; Tirrell, David A.; Zewail, Ahmed H.
- Issue Date
- NATL ACAD SCIENCES
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.107, no.40, pp.17101 - 17106
- 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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