Related Experiment Video
Updated: Aug 9, 2026

CD Spectroscopy to Study DNA-Protein Interactions
Published on: February 10, 2022
First-principles calculations of protein circular dichroism in the far-ultraviolet and beyond
Mark T Oakley1, Benjamin M Bulheller, Jonathan D Hirst
1School of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
Abstract:
Understanding the relationship between the amino acid sequence of a protein and its unique, compact three-dimensional structure is one of the grand challenges in molecular biophysics. One exciting approach to the protein-folding problem is fast time-resolved spectroscopy in the ultra-violet (UV). Time-resolved electronic circular dichroism (CD) spectroscopy offers resolution on a nanosecond (or faster) timescale, but does not provide the spatial resolution of techniques like X-ray crystallography or NMR. There is a need to underpin fast timescale spectroscopic studies of protein folding with a stronger theoretical foundation. We review some recent studies in this regard and briefly highlight how modern quantum chemical models of aromatic groups have improved the accuracy of calculations of protein CD spectra near-UV. On the other side of the far-UV, we describe calculations indicating that charge-transfer transitions are likely to be responsible for bands observed in the vacuum UV in protein CD.
More Related Videos
Related Concept Videos
Ultraviolet and Visible (UV–Vis) Spectroscopy: Overview
UV–Vis Spectroscopy: Molecular Electronic Transitions
UV–Vis Spectroscopy: Woodward–Fieser Rules
UV–Vis Spectroscopy of Conjugated Systems
One of the factors influencing λmax is the extent of conjugation in the...
UV–Vis Spectroscopy: Beer–Lambert Law
UV–Vis Spectrometers

