Dynamic Ligand-Protein Interactions Alter Rhodopsin's Conformational Ensemble: Simulations of Rhodopsin and Opsin
نویسندگان
چکیده
منابع مشابه
The Thermal Stability of Rhodopsin and Opsin
Rhodopsin, the red photosensitive pigment of rod vision, is composed of a specific cis isomer of retinene, neo-b (11-cis), joined as chromophore to a colorless protein, opsin. We have investigated the thermal denaturation of cattle rhodopsin and opsin in aqueous digitonin solution, and in isolated rod outer limbs. Both rhodopsin and opsin are more stable in rods than in solution. In solution as...
متن کاملThe Stability of Rhodopsin and Opsin
THE STABILITY OF CATTLE RHODOPSIN AND OF ITS PROTEIN MOIETY OPSIN TOWARD ACIDS AND ALKALIES AND ON AGING WAS DETERMINED BY TWO CRITERIA: maintenance of absorption spectrum, and capacity to regenerate after exposure to light. On storage at 3 degrees C. at pH near neutrality, the absorption spectrum in the visible region may remain unchanged for as long as 6 months; but the regenerability progres...
متن کاملDynamic protein ligand interactions – insights from MS
Proteins undergo dynamic interactions with carbohydrates, lipids and nucleotides to form catalytic cores, fine-tuned for different cellular actions. The study of dynamic interactions between proteins and their cognate ligands is therefore fundamental to the understanding of biological systems. During the last two decades MS, and its associated techniques, has become accepted as a method for the...
متن کاملDistinct Roles for Conformational Dynamics in Protein-Ligand Interactions.
Conformational dynamics has an established role in enzyme catalysis, but its contribution to ligand binding and specificity is largely unexplored. Here we used the Tiam1 PDZ domain and an engineered variant (QM PDZ) with broadened specificity to investigate the role of structure and conformational dynamics in molecular recognition. Crystal structures of the QM PDZ domain both free and bound to ...
متن کاملAcid-base Properties of Rhodopsin and Opsin
Purified preparations of cattle rhodopsin have been titrated to various pH, irradiated, and the pH changes followed thereafter until completed. In this way we have obtained the titration curves of rhodopsin, of the immediate product of irradiation, measured within 30 seconds; and of the final product of irradiation (opsin). The rhodopsin preparations display about 54 titratable groups per mole ...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2015
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2014.11.1434