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 well related, although not linearly, to the tyrosine/ tryptophan ratio in both model co
Study of ionization of tyrosine residues in proteins by second-derivative UV spectroscopy
โ Scribed by L. P. Breydo; A. A. Shevchenko; O. A. Kost
- Book ID
- 105596201
- Publisher
- Springer
- Year
- 1997
- Tongue
- English
- Weight
- 459 KB
- Volume
- 46
- Category
- Article
- ISSN
- 1573-9171
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Ionization of the phenolic group of N-acetyltyrosynamide has been studied using secondderivative spectroscopy. At pH 12.5 the second-derivative spectrum of the model compound revealed the presence of derivative bands in a spectral region (between 250 and 270 nm) where interference coming from other
A method for deconvolution of the near-uv second-derivative spectra of proteins into their component tryptophan, tyrosine, and phenylalanine spectra is described. In this approach, the second-derivative spectra of tryptophan and tyrosine model compounds are numerically shifted to create a set of ref