Absorption spectrum of the peptide bond: Basic properties ...

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Abstract

The basicity of a series of peptides and proteins has been determined in the sulfuric acid system and in acetic acid. The values of pKa all fall in a narrow range of values. The relation between these findings and the theory of energy transfer by peptide bonds is considered.

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☆

This study has been supported by Grant # 2848 from The National Science Foundation.

2

On leave from the Hebrew University Jerusalem, Israel.

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  Absorption in the range of 230–300 nm is dominated by the aromatic side-chains of tryptophan, tyrosine, and phenylalanine residues, and there is weak contribution by disulphide bonds near 260 nm. Crammer and Neuberger (1943) [11] and Shugar (1952) [12] were the first to use UV–Vis spectroscopy to study the optical properties of the tyrosine chromophore and to interpret changes in absorbance spectra of proteins as a function of pH. Furthermore, the UV absorption spectra of polypeptides and proteins were thoroughly investigated during the decades of 50 and 60 of the last century [13–35]. It was convenient in that time studying polypeptides and globular proteins that adopt different conformations in their folded (e.g. α-helix conformation) and unfolded states (random coil conformation) and following this transition state with UV absorption spectroscopy, optical rotatory dispersion (ORD) and circular dichroism.

• Arnett E.M.

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• Bongers J., …, Felix A.M.

  International Journal of Peptide and Protein Research • Volume 39 • 1992

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