Protein Association in Dilute and Crowded Solutions

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Please use this identifier to cite or link to this item: http://hdl.handle.net/1853/42017

Title: Protein Association in Dilute and Crowded Solutions
Author: Zhou, Huan-Xiang
Abstract: Most biological processes are mediated by mediated by protein association, and often are under kinetic rather than thermodynamic control. We have developed the transient-complex theory for protein association, which presents a framework for elucidating the mechanisms of protein association and for predicting the association rates. The transient complex refers to an intermediate along the association process, in which the two associating molecules have near-native separation and relative orientation but have yet to form the short-range specific interactions of the native complex. Our theory rationalizes the variations in association rates over 10 orders of magnitudes and gives accurate prediction of the association rates based on the structures of the native complexes. In the cellular context, association processes occur in the presence of a high concentration of background macromolecules. We have developed methods to model the effects of the crowded cellular environments on the affinities and rate constants of protein association. These studies allow us to achieve a quantitative understanding of biological processes in the cellular context, based on fundamental physical principles.
Description: Presented on November 9, 2011 from 3:00 pm to 4:00 pm In Howey building room L5. Runtime: 54:58 minutes
Type: Lecture
Video
URI: http://hdl.handle.net/1853/42017
Date: 2011-11-09
Contributor: Florida State University
Georgia Institute of Technology. School of Physics
Publisher: Georgia Institute of Technology
Subject: Physics colloquia
Protein association
Solutions
Crowded cellular environments
Kinetics

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