Course Description
This course consists of approximately seventeen 60-90 minute lectures and three 1.5 hour classes for student presentations. The first part of the course includes in-depth treatment of thermodynamics and kinetics of protein-ligand interactions and protein-protein interactions. This section also includes an introduction to the structure and function of therpeutic antibodies.
The second part of the course includes theoretical and practical aspects of biophysical methods not covered in most other courses, including surface plasmon resonance, scanning and titrating calorimetry, cryoEM, H/D exchange mass spectrometry, and other specialized methods with particular utility in modern drug discovery.
The third part of this course provides examples of theoryand methods from the first two parts, with particular emphasis on therapeutic proteins discussed, including viruses, therapeutic antibodies, bispecific antibodies, Fc-fusion proteins, and drug targets. Students are responsible for all of the material presented in the lecture notes, the classroom lectures, and, in addition, any reading material assigned by the instructors. Students will directly interact with industry scientists with expertise in biophysical analysis.
The students will understand the theoretical basis of protein-ligand interactions and current methods for their characterization. Students will be knowledgeable about current topics in the biopharmaceutical industry and the role of kinetic and thermodynamic information in the drug design process. Students will be able to critique current literature concerning therapeutically relevant proteins.
Course offered in even years.
Course Syllabus
Course lectures and notes can be found on the 528 Resources page.