Abstract

Circular Dichroism (CD) spectroscopy is a powerful and versatile technique in structural biology, providing critical insights into the conformational properties of biomolecules. By measuring the differential absorption of left- and right-handed circularly polarized light, CD spectroscopy can reveal the secondary and tertiary structures of proteins, nucleic acids, and other chiral biomolecules. This abstract explores the fundamental principles of CD spectroscopy, its application in determining protein secondary structures, monitoring conformational changes, and assessing the stability of biomolecular assemblies. It also highlights advancements in the methodology, including synchrotron radiation CD (SRCD) and computational deconvolution methods, which have significantly enhanced the sensitivity and resolution of CD analysis. The integration of CD spectroscopy with complementary techniques, such as X-ray crystallography and nuclear magnetic resonance (NMR), underscores its pivotal role in elucidating complex structural dynamics and interactions at the molecular level. Through these optical insights, CD spectroscopy continues to advance our understanding of biomolecular structure and function, paving the way for innovations in drug design, protein engineering, and synthetic biology.