Hydration dynamics at fluorinated protein surfaces

被引:61
|
作者
Kwon, Oh-Hoon [1 ,2 ]
Yoo, Tae Hyeon [1 ]
Othona, Christina M. [1 ,2 ]
Van Deventer, James A. [1 ]
Tirrell, David A. [1 ]
Zewail, Ahmed H. [1 ,2 ]
机构
[1] CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA
[2] CALTECH, Phys Biol Ctr Ultrafast Sci & Technol, Arthur Amos Noyes Lab Chem Phys, Pasadena, CA 91125 USA
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
fluorine; noncanonical amino acids; protein engineering; solvation dynamics; ultrafast hydration; NONCANONICAL AMINO-ACIDS; HUMAN SERUM-ALBUMIN; COILED-COIL; TRYPTOPHAN FLUORESCENCE; CIRCULAR-DICHROISM; SOLVATION DYNAMICS; BUNDLE PROTEIN; WATER DYNAMICS; DRIVING-FORCE; IN-VIVO;
D O I
10.1073/pnas.1011569107
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:17101 / 17106
页数:6
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