The effect of the chromophoric group modification on the optical properties of retinal proteins
Autor: | Sergei D. Varfolomeev, Pavel Kuzmichev, N. E. Belikov, E. A. Kryukova, D. A. Dolgikh, Vladimir Chupin, Peter P. Levin, Lada E. Petrovskaya, A. A. Khodonov, Alexei N. Shumsky, Alexey Lukin, Irina Melnikova, Mikhail P. Kirpichnikov, Igor Chizhov, O. V. Demina |
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Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
Proteorhodopsin genetic structures 030102 biochemistry & molecular biology biology Protein reconstitution Retinal binding Retinal Bacteriorhodopsin General Chemistry Chromophore 03 medical and health sciences chemistry.chemical_compound Pigment chemistry visual_art Biophysics biology.protein visual_art.visual_art_medium Molecule |
Zdroj: | Mendeleev Communications. 28:406-408 |
ISSN: | 0959-9436 |
Popis: | The effects of chromophoric group structures on the functional properties of bacteriorhodopsin (BR) and proteorhodopsin from E. sibiricum (ESRh) were compared. ESRh retinal binding site was found as preserving the similar stereo- and spatial restrictions on the chromophore structure during the retinal protein reconstitution process (except for C25-analog AR8). It was revealed that the structure peculiarities of the chromophore analog molecules affect the optical parameters of ESRh and BR pigment families in similar ways. |
Databáze: | OpenAIRE |
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