Protein folding: energy landscapes and molecular dynamics

This lecture explores the fundamental aspects of protein folding, from the central dogma of molecular biology to the challenges posed by Levinthal's paradox. The instructor discusses the autonomous folding of proteins, the role of thermodynamics, and the complexity of the energy landscape. Various techniques such as X-ray crystallography and Molecular Dynamics simulations are highlighted. The lecture delves into the sequence design criteria, the interplay between hydrophobic and hydrophilic amino acids, and the concept of non-equilibrium protein folding. It concludes by emphasizing the importance of understanding the relationship between protein sequence and structure, with a mention of co-evolutionary methods like alphaFold.