Steric effects of  cis ‐ trans  isomerism on neighboring residues in proline oligopeptides: A  13 C‐nmr study of conformational heterogeneity in linear tripeptides | Zendy

Deslauriers R. | Zendy; Becker J. M. | Zendy; Steinfeld A. S. | Zendy; Naider F. | Zendy

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Steric effects of cis ‐ trans isomerism on neighboring residues in proline oligopeptides: A 13 C‐nmr study of conformational heterogeneity in linear tripeptides

Author(s) -

Deslauriers R.,

Becker J. M.,

Steinfeld A. S.,

Naider F.

Publication year - 1979

Publication title -

biopolymers

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.556

H-Index - 125

eISSN - 1097-0282

pISSN - 0006-3525

DOI - 10.1002/bip.1979.360180305

Subject(s) - tripeptide , chemistry , steric effects , oligopeptide , proline , moiety , stereochemistry , peptide bond , nuclear magnetic resonance spectroscopy , residue (chemistry) , polyproline helix , cis–trans isomerism , peptide , dipeptide , chemical shift , amino acid , organic chemistry , biochemistry

A series of proline‐containing linear oligopeptides (4 dipeptides and 15 tripeptides) were synthesized and examined in aqueous and nonaqueous solutions using 13 C‐nmr spectroscopy. Spectra of linear tripeptides showing cis ‐ trans isomerism about the X ‐Pro bond ( X = Pro, Gly, and Ala) also show neighboring effects on the chemical shifts of residues both preceding and following the prolyl moiety. The extent of cis ‐ trans isomerism observed about the X ‐Pro peptide bond correlates not only with the nature of X , but also depends on the size of the residue following proline; the larger substituents favor an increase in cis content about the X ‐Pro bond.

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