NMR Studies of Protein Misfolding and Amyloid Formation
November 4, Tue 2008
1:00 pm, MRB 200 Conference Room
Dr. Kwang Hun Lim
Assistant Professor, Chemistry, East Carolina University
The process by which a polypeptide folds into a unique three-dimensional structure is one of the most fundamental problems in molecular biology. Extensive biophysical studies have shown that intra-molecular hydrogen bonding and hydrophobic interactions between the sidechains are the major driving force of protein folding. Recently, misfolded states of proteins can escape from the folding pathway and be involved in the inter-molecular hydrogen bonding and hydrophobic interaction, leading to amyloid formation. The misfolding and amyloid formation is shown to be associated with various debilitating human disease such as Alzheimer's and Parkinson's diseases. Investigation of the molecular mechanism of the misfolding and amyloid formation would, therefore, be critical to developing therapeutic strategies for amyloid diseases. Our research laboratory has been focused on characterizing the amyloidogenic state of proteins using NMR spectroscopy. Structural, dynamic properties of the amyloid-forming states and their implication for amyloid formation will be discussed in this seminar.