Protein folding is one of the most fundamental problems of the 21st century. Studies of protein folding provide a better understanding of molecular processes underlying disease which in turn helps in better drug design. These studies are complicated by the fact that the system presents innumerable degrees of freedom. The interaction of the peptide geometry determines the conformation of the peptide. The thermodynamic factors that drive high entropy (unfolded state) or low entropy (native state) of the system have to be understood in order to better understand the folding process. This work describes some of these factors and how they affect the folding process. This work presents both classical and quantum theories that explain the behavior of a molecule when perturbed by an electromagnetic radiation. It goes a head to show data from experiments demonstrating the feasibility of UV resonance Raman spectroscopy for the study of proteins.

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