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권오훈

Kwon, Oh Hoon
Ultrafast Laser Spectroscopy and Nano-microscopy Lab.
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Hydration dynamics at fluorinated protein surfaces

Author(s)
Kwon, Oh HoonYoo, Tae HyeonOthona, Christina M.Van Deventer, James A.Tirrell, David A.Zewail, Ahmed H.
Issued Date
2010-10
DOI
10.1073/pnas.1011569107
URI
https://scholarworks.unist.ac.kr/handle/201301/8730
Fulltext
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=78049299552
Citation
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.107, no.40, pp.17101 - 17106
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.
Publisher
NATL ACAD SCIENCES
ISSN
0027-8424

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