Studies of the ground and excited-state surfaces of the retinal chromophore using CAM-B3LYP
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Updated: Jun 14, 2026

Methodology for Studying Interactions of Vitamin A Membrane Receptors and Opsin Protein with their Ligands in Generating the Retinylidene Protein
Published on: October 4, 2024
Ivan V Rostov1, Roger D Amos, Rika Kobayashi
1Australian National University Supercomputer Facility, Mills Road, Canberra, ACT 0200, Australia.
Abstract:
The isomerization of the 11-cis isomer (PSB11) of the retinal chromophore to its all-trans isomer (PSBT) is examined. Optimized structures on both the ground state and the excited state are calculated, and the dependence on torsional angles in the carbon chain is investigated. Time-dependent density functional theory is used to produce excitation energies and the excited-state surface. To avoid problems with the description of excited states that can arise with standard DFT methods, the CAM-B3LYP functional was used. Comparing CAM-B3LYP with B3LYP results indicates that the former is significantly more accurate, as a consequence of which detailed cross sections of the retinal excited-state surface are obtained.
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