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Volumn 102, Issue 40, 1998, Pages 7899-7905

Protein structural changes in bacteriorhodopsin upon photoisomerization as revealed by polarized FTIR spectroscopy

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Indexed keywords


EID: 0000557270     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp981949z     Document Type: Article
Times cited : (76)

References (76)
  • 41
    • 11644288097 scopus 로고    scopus 로고
    • note
    • The error is estimated to be about 5° in the present article.
  • 55
    • 85087243830 scopus 로고    scopus 로고
    • note
    • -1 region, and all gave similar spectra.
  • 70
    • 0032540689 scopus 로고    scopus 로고
    • Recently, we have reported a novel method to introduce a cysteine residue as a hydrogen bonding probe, where we substitute Thr89 for Cys. Polarized FTIR study of the T89C mutant showed that the hydrogen bonding of the S-H group is unusually strong in the K intermediate. Similar change in the O-H group of the wild-type BR was suggested by the coincidence of the orientation of the S-H group of T89C to the O-H group of the wild-type BR. Kandori, H.; Kinoshita, N.; Shichida, Y.; Maeda, A.; Needleman, R.; Lanyi, J. K. J. Am. Chem. Soc. 1998, 120, 5828.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 5828
    • Kandori, H.1    Kinoshita, N.2    Shichida, Y.3    Maeda, A.4    Needleman, R.5    Lanyi, J.K.6
  • 72
    • 11644260301 scopus 로고    scopus 로고
    • note
    • According to the results of ref 70, the distance between the sulfur of Cys89 of T89C and the oxygen of Asp85 is likely ot become closer upon photoisomerization. This could provide one of the pieces of experimental evidence of unidirectional isomerization.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.