CD of proline-rich polypeptides: application to the study of the repetitive domain of maize glutelin-2

An overview of CD of proline-rich peptides is reported. First, structural characteristics, theoretical CD studies, and the biological relevance of polyproline II structure in such peptides are discussed. Second, a CD study of peptides belonging to the repetitive domain of maize glutelin-2, H-(Val-Hi...

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Veröffentlicht in:Biopolymers 1993-07, Vol.33 (7), p.1019-1028
Hauptverfasser: Rabanal, F, Ludevid, M.D, Pons, M, Giralt, E
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container_title Biopolymers
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creator Rabanal, F
Ludevid, M.D
Pons, M
Giralt, E
description An overview of CD of proline-rich peptides is reported. First, structural characteristics, theoretical CD studies, and the biological relevance of polyproline II structure in such peptides are discussed. Second, a CD study of peptides belonging to the repetitive domain of maize glutelin-2, H-(Val-His-Leu-Pro-Pro-Pro),-OH (n = 3, 5, 8), is described. This series of peptides displayed the CD features of polyproline II structure in water 5*C, pH 5). Moreover, it was shown that the addition of increasing amounts of the polyanionic molecule heparin forced a displacement of the conformational equilibrium of those peptides toward higher proportions of the polyproline II structure. In contrast, when the temperature is raised such a structure gradually disappears, leading to more disordered conformations
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First, structural characteristics, theoretical CD studies, and the biological relevance of polyproline II structure in such peptides are discussed. Second, a CD study of peptides belonging to the repetitive domain of maize glutelin-2, H-(Val-His-Leu-Pro-Pro-Pro),-OH (n = 3, 5, 8), is described. This series of peptides displayed the CD features of polyproline II structure in water 5*C, pH 5). Moreover, it was shown that the addition of increasing amounts of the polyanionic molecule heparin forced a displacement of the conformational equilibrium of those peptides toward higher proportions of the polyproline II structure. In contrast, when the temperature is raised such a structure gradually disappears, leading to more disordered conformations</description><subject>Amino Acid Sequence</subject><subject>Aminoacids, peptides. Hormones. 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subjects Amino Acid Sequence
Aminoacids, peptides. Hormones. Neuropeptides
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Carbohydrate Conformation
Carbohydrate Sequence
Circular Dichroism
ESPECTROMETRIA
Fundamental and applied biological sciences. Psychology
GLUTELINAS
GLUTELINE
Glutens - chemistry
Heparin - chemistry
MAIS
MAIZ
Models, Molecular
Molecular Sequence Data
Peptides - chemistry
PROLINA
PROLINE
Protein Structure, Secondary
Proteins
Repetitive Sequences, Nucleic Acid
SPECTROMETRIE
ZEA MAYS
Zea mays - chemistry
title CD of proline-rich polypeptides: application to the study of the repetitive domain of maize glutelin-2
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