Literature DB >> 15328891

Resonance energy transfer between tryptophan-214 in human serum albumin and acrylodan, prodan, and promen.

José González-Jiménez1, Manuel Cortijo.   

Abstract

It has been proposed that acrylodan (6-acryloyl-2-dimethylaminonaphthalene) and prodan (6-propionyl-2-dimethylaminonaphthalene) bind to site I of human serum albumin, whereas promen (6-propionyl-2-methoxynaphthalene) binds to site II of this carrier protein. Because human albumin contains only one single tryptophan, at position 214, it has been possible to measure the distances from this amino-acid residue to each of the three probes by nonradiative energy transfer. The distances calculated, 2.97 +/- 0.10 nm, 3.14 +/- 0.11 nm, and 2.62 +/- 0.17 nm, respectively, confirm the locations previously proposed for all three probes.

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Year:  2004        PMID： 15328891     DOI： 10.1023/b:jopc.0000032655.26249.ba

Source DB:  PubMed          Journal:  Protein J        ISSN： 1572-3887            Impact factor:   2.371


  22 in total

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Authors:  F Moreno; M Cortijo; J González-Jiménez
Journal:  Photochem Photobiol       Date:  1999-11       Impact factor: 3.421

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Authors:  J Gonzalez-Jimenez; G Frutos; I Cayre; M Cortijo
Journal:  Biochimie       Date:  1991-05       Impact factor: 4.079

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Journal:  Biochem J       Date:  1989-02-15       Impact factor: 3.857
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  4 in total

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4.  Solvent and pH effects on the fluorescence of 7-(dimethylamino)-2-fluorenesulfonate.

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  4 in total

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