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Conformational analysis of the repeated sequence of glutelin‐2, a maize storage protein
Author(s) -
Pons Miquel,
Feliz Miguel,
Celma Carles,
Giralt Ernest
Publication year - 1987
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1260250504
Subject(s) - polyproline helix , chemistry , glutelin , random coil , hydrogen bond , storage protein , histidine , residue (chemistry) , proline , stereochemistry , circular dichroism , peptide , amino acid , molecule , organic chemistry , biochemistry , gene
Abstract The presence of repeated proline‐rich sequences constitutes a common trend in several cereal storage proteins. The protected hexapeptide Boc‐Val‐His‐Leu‐Pro‐Pro‐Pro‐OH (1), with the sequence of the repeated region of glutelin‐2 (28 kD) from maize, has been studied by proton and 13 C NMR in D 2 O, DMSO‐d 6 , CDCl 3 and CDCl 3 ‐CD 3 OD at different temperatures. Spectra were assigned mainly by using 2D correlation techniques. The spectra in D 2 O and DMSO‐ d 6 suggest that peptide 1 has a random coil, all‐ trans conformation. In CDCl 3 1 presents a folded conformation, stabilized by hydrogen bonds, with one of the methyl groups of the valine residue situated over the histidine ring. In CDCl 3 ‐CD 3 OD 1 is present as a mixture of different conformations. The spectral data are discussed taking as a reference the known conformation of polyproline.