Circular dichroism (CD) spectrometer is a powerful tool to compare the relative structure content and thermal stability of proteins and nucleic acid samples in solution. The instrument is currently configured to:

• Estimate the secondary structure content of proteins or nucleic acids: CD spectra have typical shapes for alpha-helical, beta-sheet, unfolded proteins and nucleic acids.
• Measure the thermodynamic stability of a protein or nucleic acid sample from a temperature or chaotrope mediated melting curve.
• Demonstrate similar fold and stability of protein samples that carry point mutations, which fulfills new NIH guidelines on Transparency and Reproducibility.
• Compare structure and thermal stability of phylogenetically-related, alternatively spliced, post-transcriptionally or post-translationally-modified protein samples.
• Measure association or dissociation kinetics of protein-protein, protein-ligand, and nucleic acid ligand interactions, depending upon the conformational changes observed in biomolecular complexes.