Work

Hydration dynamics at fluorinated protein surfaces

Year: 2010

Type: article

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.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.1011569107

Authors: Oh-Hoon Kwon, Tae Hyeon Yoo, Christina M. Othon, James A. Van Deventer, David A. Tirrell, Ahmed H. Zewail

Institutions: California Institute of Technology, Wesleyan University

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Awards: G5594773905, New Amino Acids for Protein Engineering