CAREER: Probing the Early Folding Dynamics and Folding Energy Landscape

University Of Pennsylvania, Philadelphia PA

Investigators

Abstract

Professor Feng Gai of the University of Pennsylvania is supported by the Experimental Physical Chemistry CAREER program to study protein folding dynamics. The principal objective of this work is to study protein spontaneous fluctuations and folding dynamics at both single molecule and ensemble levels. Laser-induced temperature-jump methods for rapid refolding/unfolding initiation and two-dimensional time-resolved infrared correlation and fluorescence spectroscopies, some in confocal geometries, will be used to study the early folding events. Secondary structure formation in alanine-based helical peptides, helix-helix interation in GCN4-p1 and other helical bundles, and the folding mechanism of an all-beta-sheet protein, the E. Coli major cold shock protein A, will be studied. Isotope editing will be used in order to achieve high structural resolution. Many modern biophysical techniques are appropriate for undergraduate research. The PI plans to include undergraduates in this work, and also will be involved in public science education through special summer programs designed for local high school students at the University of Pennsylvania.