Related Experiment Video
Updated: Jul 15, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Comparative photophysics and ultrafast dynamics of dimethylaminochalcone and a structurally rigid derivative:
1Radiation and Photochemistry Division, Bhabha Atomic Research Centre, Mumbai 400085, India. rajchem06@gmail.com.
Abstract:
Photophysical parameters and ultrafast dynamics of dimethylaminochalone (DMAC-A) have been compared with a structurally bridged analogue (namely, c-DMAC) in solvents of varying polarities. Conformational locking of the single bond connecting the donor and acceptor groups in c-DMAC arrests the twisted intramolecular charge transfer (TICT) relaxation and consequently the photophysical parameters such as fluorescence yield, fluorescence lifetime and triplet yield change significantly. The intramolecular charge transfer character of the LE state is found to be unaffected by conformational restriction. Femtosecond transient absorption spectroscopic studies confirmed that in polar solvents, solvation is the only relaxation process in c-DMAC as opposed to the ultrafast TICT of DMAC-A. The solvent polarity effect on the relaxation dynamics has also been discussed.
More Related Videos
10:35Novel Techniques for Observing Structural Dynamics of Photoresponsive Liquid Crystals
Published on: May 29, 2018
08:54Vibrational Spectra of a N719-Chromophore/Titania Interface from Empirical-Potential Molecular-Dynamics Simulation, Solvated by a Room Temperature Ionic Liquid
Published on: January 25, 2020
Related Concept Videos
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
UV–Vis Spectroscopy: Woodward–Fieser Rules