Folding Dynamics of Single GCN-4 Peptides by Fluorescence Resonant Energy Transfer Confocal Microscopy
Document Type
Article
Publication Date
8-1-1999
Abstract
We have prepared a bichromophoric crosslinked variant of GCN4-P1 for single-molecule fluorescence energy transfer experiments (GCN4-Pf). The folding and unfolding fluctuations of single GCN4-Pf molecules are measured in a two-channel confocal microscope with which donor and acceptor fluorescence trajectories are measured simultaneously. The energy transfer efficiency is thereby determined and its probability distributions as a function of added denaturant [urea] are calculated. The distributions indicate that single molecule GCN4-Pf is in dynamic folding equilibrium with the position of the equilibrium being altered by the concentration of urea.
DOI
10.1016/S0301-0104(99)00127-5
Montclair State University Digital Commons Citation
Jia, Yiwei; Talaga, David; Lau, Wai Leung; Lu, Helen S.M.; DeGrado, William F.; and Hochstrasser, Robin M., "Folding Dynamics of Single GCN-4 Peptides by Fluorescence Resonant Energy Transfer Confocal Microscopy" (1999). Department of Chemistry and Biochemistry Faculty Scholarship and Creative Works. 469.
https://digitalcommons.montclair.edu/chem-biochem-facpubs/469