Ontology highlight
ABSTRACT:
SUBMITTER: Kwon OH
PROVIDER: S-EPMC2951393 | biostudies-other | 2010 Oct
REPOSITORIES: biostudies-other
Kwon Oh-Hoon OH Yoo Tae Hyeon TH Othon Christina M CM Van Deventer James A JA Tirrell David A DA Zewail Ahmed H AH
Proceedings of the National Academy of Sciences of the United States of America 20100920 40
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 ultrafas ...[more]