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

✍ Scribed by M. H. Baron; C. De Loze; C. Toniolo; G. D. Fasman

Publisher
Wiley (John Wiley & Sons)
Year
1978
Tongue
English
Weight
739 KB
Volume
17
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

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.

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