The role of hydroxyproline in collagen folding: Conformational energy calculations on oligopeptides containing proline and hydroxyproline

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The role of hydroxyproline in collagen folding: conformational energy calculations on oligopeptides containing proline and hydroxyproline.

We have observed that the rate of folding of the enzymatically hydroxylated form of poly(G1yPro-Pro) into the triple-helical conformation is considerably higher than that of the unhydroxylated polypeptide [R. K. Chopra and V. S. Ananthanarayanan (1982) Proc. Nutl. Acud. Sci. USA 79, 7180-71841. In this study, we examine a plausible kinetic pathway for triple-helix formation by selecting peptide...

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Conversion of proline to hydroxyproline and its incorporation into collagen.

Most, if not all, of the hydroxyproline in collagen appears to be derived from proline (1, 2). It has been proposed by several investigators (2-7), on indirect evidence, that it is a bound form of proline which is hydroxylated and incorporated into collagen. Recent data (8-11) indicate an analogous situation in the hydroxylation of lysine and its incorporation into collagen. The type of compoun...

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Rapid robust separation of hydroxyproline and proline.

The presence of hydroxyproline, and the determination of the ratio of the secondary amino acids proline to hydroxyproline, in amino acid hydrolysates specifically identifies collagen and collagen peptides. o-Phthalaldehyde, and then 9-fluorenylmethyl chloroformate, were used to carry out sequential prederivatization of amino acid hydrolysates in an in-line high-performance liquid chromatography...

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ژورنال

عنوان ژورنال: Biopolymers

سال: 1988

ISSN: 0006-3525,1097-0282

DOI: 10.1002/bip.360270209