Related Experiment Video
Updated: Jun 12, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Simulation study of chiral two-dimensional ultraviolet spectroscopy of the protein backbone
Darius Abramavicius1, Jun Jiang, Benjamin M Bulheller
1Department of Chemistry, University of California, Irvine, California, USA.
Abstract:
Amide n-pi* and pi-pi* excitations around 200 nm are prominent spectroscopic signatures of the protein backbone, which are routinely used in ultraviolet (UV) circular dichroism for structure characterization. Recently developed ultrafast laser sources may be used to extend these studies to two dimensions. We apply a new algorithm for modeling protein electronic transitions to simulate two-dimensional UV photon echo signals in this regime and to identify signatures of protein backbone secondary (and tertiary) structure. Simulated signals for a set of globular and fibrillar proteins and their specific regions reveal characteristic patterns of helical and sheet secondary structures. We investigate how these patterns vary and converge with the size of the structural motif. Specific chiral polarization configurations of the UV pulses are found to be sensitive to aspects of the protein structure. This information significantly augments that available from linear circular dichroism.
Related Concept Videos
Ultraviolet and Visible (UV–Vis) Spectroscopy: Overview
UV–Vis Spectroscopy of Conjugated Systems
One of the factors influencing λmax is the extent of conjugation in the...
UV–Vis Spectroscopy: Molecular Electronic Transitions
2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)
IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration
According to Hooke's law, the vibrational frequency is directly proportional to the...
UV–Vis Spectroscopy: Woodward–Fieser Rules

