Literature DB >> 6722128

Determination of tyrosine exposure in proteins by second-derivative spectroscopy.

R Ragone, G Colonna, C Balestrieri, L Servillo, G Irace.   

Abstract

The mutual interference between the second-derivative bands of tyrosine and tryptophan in proteins has been evaluated in terms of the ratio r between two peak to peak distances. The r values have been found to be not only related to the tyrosine/tryptophan ratio but also dependent on the polarity of the medium in which tyrosyl residues are embedded. The results obtained on purified proteins have been found consistent with the available X-ray information and with the existing solvent perturbation data.

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Year:  1984        PMID： 6722128     DOI： 10.1021/bi00303a044

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


  36 in total

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9.  High-pressure refolding of bikunin: efficacy and thermodynamics.

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