Speaker
Stefan Wallin
(Memorial University of Newfoundland)
Description
The traditional view holds that proteins fold into essentially unique and stable 3-dimensional structures which, in turn, determine their biological functions. Evidence is mounting, however, for a pervasive role of large-scale conformational changes for how proteins carry out their functions. Examples include the ability of some proteins to switch between entirely different folded structures, and the disorder-order transitions exhibited by so-called intrinsically disordered proteins. I will introduce a coarse-grained approach that allows the physics of such conformational switching in proteins to be studied on the computer. The approach is characterized by an intermediate level of geometric detail and a procedure for determining effective model parameters based on the properties of proteins’ global free energy landscapes. I will discuss the implications of our results for the mechanisms underlying molecular recognition and the evolution of new protein folds.
Primary author
Stefan Wallin
(Memorial University of Newfoundland)
