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Titolo:
Studies of chromophore retinal structure in bacteriorhodopsin by double-beam Fourier transform spectroscopy
Autore:
Terpugov, EL; Viskovatykh, AV; Degtyareva, OV; Fesenko, EE;
Indirizzi:
RussianaAcad Sci, Inst Cell Biophys, Pushchino 142292, Moscow Region, Russi Russian Acad Sci Pushchino Moscow Region Russia 142292 scow Region, Russi Russian Acad Sci, Cent Bur Unique Instrumentat, Moscow 117342, Russia Russian Acad Sci Moscow Russia 117342 nstrumentat, Moscow 117342, Russia
Titolo Testata:
BIOFIZIKA
fascicolo: 6, volume: 43, anno: 1998,
pagine: 1002 - 1011
SICI:
0006-3029(199811/12)43:6<1002:SOCRSI>2.0.ZU;2-B
Fonte:
ISI
Lingua:
RUS
Soggetto:
INFRARED DIFFERENCE SPECTROSCOPY; RESONANCE RAMAN-SPECTROSCOPY; DRIVEN PROTON PUMP; HALOBACTERIUM-HALOBIUM; PRIMARY PHOTOCHEMISTRY; PURPLE MEMBRANES; MECHANISM; CYCLE;
Keywords:
FT-IR-spectroscopy; bacteriorhodopsin; dehydration;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Terpugov, EL RussianaAcad Sci, Inst Cell Biophys, Pushchino 142292, MoscowRegion, Russi Russian Acad Sci Pushchino Moscow Region Russia 142292 Russi
Citazione:
E.L. Terpugov et al., "Studies of chromophore retinal structure in bacteriorhodopsin by double-beam Fourier transform spectroscopy", BIOFIZIKA, 43(6), 1998, pp. 1002-1011

Abstract

A new approach to studying chromophore-containing proteins is described, which is based on double-beam Fourier transform spectroscopy. It is shown that dehydration changes the structure of the retinal of light-adapted purplemembranes. Absorption spectra in infrared for the retinal of native bacteriorhodopsin (BR568), the first intermediate of the photocycle (K-610), and the form BR506 in dry films were obtained. The spectra shown many new features compared with resonance Raman and FT-IR difference spectra.

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Documento generato il 29/11/20 alle ore 09:52:43