Project 16926 simulates a very small model system: alanine tetrapeptide. Alanine is one of twenty amino acids that make up all proteins. Although polyalanine is predominantly in the alpha-helical conformation in solution, there are many competing conformations that the peptide chain must search before folding.
This project aims to statistically sample folding trajectories of alanine tetrapeptide, to help us develop new ways of performing adaptive sampling simulations that can accelerate the conformational search. Although this is a simple model system, we hope that the insights obtained will help us develop new and improved ways of performing adaptive sampling of protein-ligand interactions, to better screen potential therapeutics.
List of Contributors
This project is managed by Prof. Vincent Voelz at Temple University.
Dr. Voelz's research focuses on using new simulation methods to unravel the mysteries of how proteins self-assemble into their functional folds, and to design folding and binding properties of proteins and peptide mimetics from first principles. The Voelz Lab participates in the Folding@home project, hosting two servers at Temple University. Dr. Voelz was formerly a postdoctoral scholar in the Vijay Pande lab at Stanford University.
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