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Volumn 101, Issue 49, 1997, Pages 10542-10547

Infrared difference spectra of the intermediates L, M, N, and O of the bacteriorhodopsin photoreaction obtained by time-resolved attenuated total reflection spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

BAND STRUCTURE; FOURIER TRANSFORM INFRARED SPECTROSCOPY; PH EFFECTS; PHOTOCHEMICAL REACTIONS; PROTEINS; THERMAL EFFECTS;

EID: 0031553201     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp971047i     Document Type: Article
Times cited : (99)

References (41)
  • 19
    • 4243151018 scopus 로고    scopus 로고
    • note
    • The transient pH change along the purple membrane surface due to proton pumping by BR is smaller than 0.2 pH units in an unbuffered suspension (calculated from data of ref 4). The change in bulk medium pH is only 0.05. Although the ability of the used buffers to diffuse between the purple membrane sheets is not precisely known, the small pH change by proton pumping will be decreased by the buffer. This rules out any large effects on the photocycle kinetics. The chemical nature and the concentration of the buffers used do not influence the photoreaction (cf. ref 4).
  • 32
    • 4243112125 scopus 로고    scopus 로고
    • note
    • It should be stressed at this point that due to different polarization conditions the ATR technique is more sensitive to changes in the amide I modes of α-helixes than transmission spectroscopy (cf. ref 15).
  • 37
  • 40
    • 4243085080 scopus 로고    scopus 로고
    • note
    • 41 published O-BR difference spectra of E204 mutants. The close agreement of their spectra with those presented here (Figure 4) confirms our findings. Minor differences may be explained by using different techniques (ATR, transmission) and different measuring conditions (pH, temperature, time) and by the lower signal-to-noise ratio of the difference spectra of Kandori et al.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.