Ultraviolet absorption spectra of peptides. II. Glycine peptides containing more than one substituted amide link
1955; Elsevier BV; Volume: 56; Issue: 1 Linguagem: Inglês
10.1016/0003-9861(55)90332-5
ISSN1096-0384
Autores Tópico(s)Photoreceptor and optogenetics research
Resumo1. Spectra in the ultraviolet region from about 200 to 240 mμ are presented for aqueous solutions at various pH values for H.Glyn.OH, where n = 2, 3, 4, 5, and 6, for glycine anhydride, H.Ala-Gly2.OH, H. Leu-Gly2.OH, Ac-Phe-Gly. OH, and Ac-Phe-Gly2.OH. Also the spectrum of a preparation of polyglycine methyl ester in 43% H3PO4 is presented. 2. Evidence is presented to show that the spectrum of an individual peptide link within a peptide containing more than one peptide link is influenced by the presence of adjacent peptide links. 3. The attempt is made to show that it may be possible to assign to each of the endoresidues in a short peptide chain individual residue spectra which are additive no matter what the sequence of residues is in the chain. The rational basis for this hypothesis is discussed. The main evidence for it is based upon the observation that at pH's 1 and 6 there appears to be an approximately constant difference between the spectra of a number of pairs of peptides which differ from each other only by a single endoglycine residue. Extension of the above principle to macromolecules is briefly discussed.
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