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Published October 5, 2010 | Supplemental Material + Published
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Hydration dynamics at fluorinated protein surfaces


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.

Additional Information

© 2010 National Academy of Sciences. Contributed by David A. Tirrell, August 4, 2010 (sent for review May 10, 2010). We thank Prof. Thomas Miller for helpful discussion, J.D. Fisk for synthesis of homoisoleucine, and the referees for their thoughtful comments on the original manuscript. This work is supported by National Institutes of Health (NIH) Grant GM62523, National Science Foundation (NSF) Grant DMR-0964886, Office of Naval Research (ONR) Grant N00014-03-1-0793, a Samsung Scholarship (to T.H.Y.), and a National Defense Science and Engineering Graduate Fellowship (to J.A.V.D.). Author contributions: O.-H.K., T.H.Y., C.M.O., J.A.V.D., D.A.T., and A.H.Z. designed research; O.-H.K., T.H.Y., C.M.O., J.A.V.D., D.A.T., and A.H.Z. performed research; O.-H.K., T.H.Y., C.M.O., J.A.V.D., D.A.T., and A.H.Z. analyzed data; and O.-H.K., T.H.Y., C.M.O., J.A.V.D., D.A.T., and A.H.Z. wrote the paper. O.-H.K. and T.H.Y. contributed equally to this work. The authors declare no conflict of interest. This article contains supporting information online at www.pnas.org/lookup/suppl/doi:10.1073/pnas.1011569107/-/DCSupplemental.

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Published - Kwon2010p11624P_Natl_Acad_Sci_Usa.pdf

Supplemental Material - pnas.1011569107_SI.pdf


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