The Hierarchy of Protein Folding
Abstract
Proteins are biological macromolecules composed of linear polypeptide chains. Often, a specific three-dimensional arrangement of the constituting polypeptide chains is required to provide the protein a biological function. Despite all the advancements in protein science, a simple, yet fundamental question remains: How do proteins fold so quickly? A polypeptide chain has near infinite conformational space, yet many proteins are capable of rapidly navigating from a structureless state to their native conformation on the order of milliseconds to seconds. Therefore, it is clear that proteins cannot exhaustively probe their entire conformational space, and instead must somehow explore a more limited conformational space as they fold.
This presentation will provide an introduction to the concepts involved in protein folding. It will cover the underlying physical forces governing folding, the experimental evidence used to understand the folding behavior of proteins on a macroscopic and microscopic scale, and how the microscopic behavior of proteins can circumvent the time-scale folding problem.
About the speaker
Remi Casier obtained his BSc in honours chemistry in 2013 followed by his MSc in polymer chemistry in 2015 from the University of Waterloo. Under the supervision of Prof. Jean Duhamel, Remi is currently pursuing his PhD in polymer science. Currently, his research focuses on using advanced fluorescence techniques to probe the conformational state and internal dynamics of polypeptides in solution in order to provide insight to the dynamic behavior of proteins.