Isomerization kinetics of N-acetyl-3-fluoro-D-proline O-methyl esters

BIOL 38

Colin A Thomas, colin.thomas@wichita.edu, ER. Talaty, talaty@twsuvm.uc.twsu.edu, and James Bann, jim.bann@wichita.edu. Department of Chemistry, Wichita State University, 1845 N. Fairmount, Wichita, KS 67260-0051
Proline residues are known to adopt both cis and trans conformations in native proteins, and the cis/trans isomerization of proline peptidyl bonds is thought to play a role in the folding/unfolding mechanisms. Two fluorine labeled enantiomers, N-acetyl-(3R)-3-fluoroproline methyl ester and N-acetyl-(3S)-3-fluoroproline methyl ester have been prepared, and the isomerization kinetics have been determined using dynamic NMR measurements. By incorporating these 19F labeled prolines into proteins, information regarding the kinetic control that cis/trans isomerization of proline plays in protein folding may be easily observed.