Principles of Biomolecular Spectroscopy

3 units

This course focuses on the core principles of biomolecular spectroscopy and how photon–protein interactions across wavelengths reveal a molecule’s structure, conformation, and dynamics. Students will explore the physical foundations of spectroscopic methods, including UV–Vis, fluorescence, circular dichroism, infrared, Raman, X-ray, and emerging techniques. They will learn how each technique targets specific structural features, secondary, tertiary, and quaternary, and how environmental changes, folding, and ligand binding produce characteristic spectral signals. The curriculum integrates spectroscopy with biophysical concepts related to stability, folding landscapes, and conformational behavior. Industry-relevant applications span biotherapeutics, diagnostics, formulation, and process monitoring. Eight modules using the Python-based visualization software PyMOL, combined with five practical labs, provide hands-on experience in data collection and interpretation of structure-spectrum relationships. Additionally, two to three lectures will cover transformer-based ML methods for the de novo design and development of biomolecules, as well as the engineering of natural proteins for advanced functions. The course will devote two modules to translation challenges, regulatory considerations (FDA), validation, data integrity, and pathways for industry deployment. The course is designed for undergraduates with an interest in biomolecular research and a willingness to engage with both theory and practical data analysis, with the expectation that students will develop the skills to design spectroscopic experiments, interpret results in structural terms, and consider regulatory implications for real-world applications.