Solvent and protein effects on the structure and dynamics of the rhodopsin chromophore.

Détails

ID Serval
serval:BIB_0DCD05E43C72
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Solvent and protein effects on the structure and dynamics of the rhodopsin chromophore.
Périodique
ChemPhysChem
Auteur(s)
Röhrig U.F., Guidoni L., Rothlisberger U.
ISSN
1439-4235 (Print)
ISSN-L
1439-4235
Statut éditorial
Publié
Date de publication
2005
Peer-reviewed
Oui
Volume
6
Numéro
9
Pages
1836-1847
Langue
anglais
Résumé
The structure and dynamics of the retinal chromophore of rhodopsin are investigated systematically in different environments (vacuum, methanol solution, and protein binding pocket) and with different computational approaches (classical, quantum, and hybrid quantum mechanics/molecular mechanics (QM/MM) descriptions). Finite temperature effects are taken into account by molecular dynamics simulations. The different components that determine the structure and dynamics of the chromophore in the protein are dissected, both in the dark state and in the early photointermediates. In vacuum and in solution the chromophore displays a very high flexibility, which is significantly reduced by the protein environment. In the 11-cis chromophore, the bond-length alternation, which is correlated with the dipole moment, is found to be similar in solution and in the protein, while it differs greatly with respect to minimum-energy vacuum structures. In the model of the earliest protein photointermediate, the highly twisted chromophore shows a very reduced bond-length alternation.
Mots-clé
Molecular Structure, Proteins/chemistry, Quantum Theory, Rhodopsin/chemistry, Solvents/chemistry, Thermodynamics
Pubmed
Web of science
Création de la notice
30/10/2015 10:10
Dernière modification de la notice
03/03/2018 13:40
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