Structure in solution of protected homo-oligopeptides ofL-valine,L-isoleucine, and L-phenylalanine: An infrared absorption study

Autor: M.H. Baron, Gerald D. Fasman, Claudio Toniolo, C. de Loze
Rok vydání: 1978
Předmět:
Zdroj: Biopolymers. 17:2225-2239
ISSN: 1097-0282
0006-3525
DOI: 10.1002/bip.1978.360170915
Popis: Monodisperesed, N-and C-Protected homo-oligopeptides [number (n) of resides from 2 to 5] of L-valine, L-isoleucine, and L-phenylalnine were studied by ir absorption spectroscopy between 1200 and 350 cm−1 at various solvents. The solvents and chain-length effects were examined for non-hydrogen-bonded peptide groups. The frequencies of the self-associated species are consistent with a model derived from the amide data. Self-association species are consistent with a model derived from the amide data. Self-association is favored by higher values of n = 2, the peptide is insoluble when more than two chains are bonded. For n = 3, 4, several chains may be associated by sliding along one another and remain soluble. For n = 2, the peptide is insoluble when more than two chains are bonded. For n = 3, 4, several chains may be associated by sliding along one another and remain slouble. For n = 5, the effect of n is to favour a model in which two chains exactly face each other so that the peptide precipitates at relatively low concentration.
Databáze: OpenAIRE
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