The roles of proteins is directly related to their three-dimensional structure and the atomic positions of the amino acids that make up their structures. This course covers the molecular details of how polypeptide chains form these remarkable shapes. The different theories of how proteins fold in vitro and in vivo, and the experimental basis for these theories will be discussed. The course also covers structure prediction/modeling from amino acid sequence, to experimental analysis by a variety of biophysical methods including electron microscopy, NMR, and X-ray crystallography. Particular case studies will be used to study the relationship between structure and function. The course content will include current approaches to the treatment of disease by using rational drug design and manipulating the structure of proteins in order to alter their function.

Biophysical and Crystal Structure analysis of Proteins
This course will follow the entire process involved in solving the crystal structure of a protein, from choosing a protein to study to using the crystal structure for structure/function studies. Topics will include: molecular cloning and expression/purification of proteins,  biophysical analysis of the purified protein, which will include discussion of analytical ultracentrifugation, static and dynamic light scattering, mass spectrometry, circular dichroism, and a brief discussion of NMR methods, and the theory and practice of crystallography. While the theory behind the steps involved in solving a crystal structure will be discussed, more emphasis will be placed on understanding the principles and purpose of each step.