Infrared and Raman study in the solid state of fully protected, monodispersed homooligopeptides ofL-valine,L-isoleucine, andL-phenylalanine

Autor:	Claudio Toniolo, Gerald D. Fasman, C. de Loze, M.H. Baron
Rok vydání:	1979
Předmět:	Dipeptide Infrared Stereochemistry Chemistry Organic Chemistry Biophysics Phenylalanine General Medicine Antiparallel (biochemistry) Biochemistry Spectral line Biomaterials chemistry.chemical_compound symbols.namesake Deuterium Valine symbols Raman spectroscopy
Zdroj:	Biopolymers. 18:411-424
ISSN:	1097-0282 0006-3525
DOI:	10.1002/bip.1979.360180216
Popis:	An ir-absorption and Raman-scattering study, in the solid state, has been carried out on monodispersed, N- and C-protected homooligopeptides (number of residues, n, from 2 to 7) of L-valine, L-isoleucine, and L-phenylalanine. The amide I, II, III, V, and vNH regions have been examined. Some deuterated (ND) samples have been examined to complete the assignments. L-Phenylalanine dipeptide displays spectral characteristics compatible with the parallel β-structure; L-isoleucine and L-valine dipeptides are probably in a distorted structure. A mixture of parallel and antiparallel extended chains cannot be excluded for the peptides with n = 3. In the amide I region the spectra of peptides with n ≥ 4 show the existence of the β-conformation. The problem of chain orientation within the pleated-sheet structure is discussed on the basis of a recent theoretical treatment of vibrational interactions of the amide I mode.
Databáze:	OpenAIRE
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