Literature DB >> 4089036

Alkaline quenching of bacteriorhodopsin tryptophanyl fluorescence: evidence for aqueous accessibility or a hydrogen-bonded chain.

P L Palmer, W V Sherman.   

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Year:  1985        PMID： 4089036     DOI： 10.1111/j.1751-1097.1985.tb01607.x

Source DB:  PubMed          Journal:  Photochem Photobiol        ISSN： 0031-8655            Impact factor:   3.421


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  5 in total

1.  Energy transfer from tryptophane amino acid residues to retinal in a bacteriorhodopsin molecule within a femtosecond timescale.

Authors:  O A Dzhemesyuk; S A Antipin; F E Gostev; I B Fedorovich; O M Sarkisov; M A Ostrovskii
Journal:  Dokl Biochem Biophys       Date:  2002 Jan-Feb       Impact factor: 0.788

2.  Independent photocycles of the spectrally distinct forms of bacteriorhodopsin.

Authors:  Z Dancsházy; R Govindjee; T G Ebrey
Journal:  Proc Natl Acad Sci U S A       Date:  1988-09       Impact factor: 11.205

3.  Decay of the tryptophan fluorescence anisotropy in bacteriorhodopsin and its modified forms.

Authors:  R van den Berg; D J Jang; M A el-Sayed
Journal:  Biophys J       Date:  1990-04       Impact factor: 4.033

4.  Tryptophan fluorescence quenching as a monitor for the protein conformation changes occurring during the photocycle of bacteriorhodopsin under different perturbations.

Authors:  D J Jang; M A el-Sayed
Journal:  Proc Natl Acad Sci U S A       Date:  1989-08       Impact factor: 11.205

5.  Effects of tryptophan mutation on the deprotonation and reprotonation kinetics of the Schiff base during the photocycle of bacteriorhodopsin.

Authors:  S Wu; Y Chang; M A el-Sayed; T Marti; T Mogi; H G Khorana
Journal:  Biophys J       Date:  1992-05       Impact factor: 4.033
  5 in total

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