Protein Folding: Structure and Design

This lecture delves into the biophysics of protein folding, exploring the intricate process of how proteins achieve their native state to perform biological functions. The instructor discusses the challenges of protein folding, the role of hydrophobic interactions, and the concept of compact conformations. The lecture also covers the HP model, which simplifies protein sequences to hydrophobic (H) and polar (P) amino acids. Furthermore, it touches upon the importance of co-evolution in understanding protein structures and sequences, as well as the integration of experimental and evolutionary information in computational protein folding methods.