Perceived for many years as a low-resolution biophysical technique, circular dichroism (CD) spectroscopy has advanced well beyond its conventional textbook description. This white paper highlights the expanding role of CD as it undergoes a fundamental transition from its origins in basic academic research to becoming an indispensable tool for the biopharmaceutical industry—a biophysical characterization technique that offers far more than the proportion of α-helix and β-sheet in a protein.
- Near-UV circular dichroism spectra reveal minor changes in tertiary structure, complementing the traditional use of far-UV scans to detect change in secondary structure
- Objective, statistically-validated higher order structure (HOS) comparisons of circular dichroism spectra confirm similarities or differences between samples, replacing subjective, visual comparisons
- Comprehensive information about structure and stability is revealed in a single continuous, multi-wavelength thermal denaturation experiment
In short, state-of-the-art CD analysis provides unique insights into changes in secondary and tertiary structure, as well as kinetic and thermodynamic information, enabling researchers to publish with confidence and contributing to informed decision-making during biotherapeutic development.