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Hydration dynamics at fluorinated protein surfaces

Kwon, Oh-Hoon and Yoo, Tae Hyeon and Othon, Christina M. and Van Deventer, James A. and Tirrell, David A. and Zewail, Ahmed H. (2010) Hydration dynamics at fluorinated protein surfaces. Proceedings of the National Academy of Sciences of the United States of America, 107 (40). pp. 17101-17106. ISSN 0027-8424. PMCID PMC2951393. http://resolver.caltech.edu/CaltechAUTHORS:20101026-075632113

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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.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1073/pnas.1011569107 DOIArticle
http://www.pnas.org/content/107/40/17101.abstractPublisherArticle
http://www.pnas.org/lookup/suppl/doi:10.1073/pnas.1011569107/-/DCSupplementalPublisherSupporting Information
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2951393/PubMed CentralArticle
ORCID:
AuthorORCID
Tirrell, David A.0000-0003-3175-4596
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.
Funders:
Funding AgencyGrant Number
NIHGM62523
NSFDMR-0964886
Office of Naval Research (ONR)N00014-03-1-0793
SamsungUNSPECIFIED
National Defense Science and Engineering Graduate (NDSEG) FellowshipUNSPECIFIED
Subject Keywords:fluorine; noncanonical amino acids; protein engineering; solvation dynamics; ultrafast hydration
PubMed Central ID:PMC2951393
Record Number:CaltechAUTHORS:20101026-075632113
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20101026-075632113
Official Citation:Oh-Hoon Kwon, Tae Hyeon Yoo, Christina M. Othon, James A. Van Deventer, David A. Tirrell, and Ahmed H. Zewail Hydration dynamics at fluorinated protein surfaces PNAS 2010 107 (40) 17101-17106; published ahead of print September 20, 2010, doi:10.1073/pnas.1011569107
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:20519
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:19 Nov 2010 23:15
Last Modified:03 Aug 2016 19:16

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