Folding Dynamics of Single GCN-4 Peptides by Fluorescence Resonant Energy Transfer Confocal Microscopy

Authors

Yiwei Jia, Olympus CorporationFollow
David Talaga, Montclair State UniversityFollow
Wai Leung Lau, University of PennsylvaniaFollow
Helen S.M. Lu, University of Pennsylvania
William F. DeGrado, University of California at San FranciscoFollow
Robin M. Hochstrasser, University of Pennsylvania

Document Type

Article

Publication Date

8-1-1999

Journal / Book Title

Chemical Physics

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.

Comments

This article is Open Access and distributed under a Creative Commons 4.0 license.

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