Journal ArticleDOI
Hydroxyproline content and location in relation to collagen thermal stability
TLDR
The results agree with the idea that the influence exerted by proline and hydroxyproline on the stabilization of the triple helix of collagen is different.Abstract:
A new analysis has been made on studies of the influence of imino acid content on the changes of collagen thermal stability (tm). It is shown that, for the interstitial vertebrate collagens, there is a strict regularity in the changes of tm depending on hydroxyproline content. No correlation is observed between tm and proline content. Also, no correlation between tm and hydroxyproline content is observed for invertebrate and basement membrane collagens. On the basis of the reported data, the dependence of tm on hydroxyproline content is considered to be not a correlation between tm and the total content of hydroxyproline, but only as the correlation between tm and the content of hydroxyproline occurring at the third position in the sequence (Gly-R2-R3)n. The results agree with the idea that the influence exerted by proline and hydroxyproline on the stabilization of the triple helix of collagen is different.read more
Citations
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Journal ArticleDOI
Functional and bioactive properties of collagen and gelatin from alternative sources: A review
TL;DR: The present work is a compilation of recent information on collagen and gelatin extraction from new sources, as well as new processing conditions and potential novel or improved applications, many of which are largely based on induced cross-linking, blending with other biopolymers or enzymatic hydrolysis.
Book ChapterDOI
Stability of proteins. Proteins which do not present a single cooperative system
TL;DR: The practical importance of thermodynamic studies of protein stability—that is, its importance not only for understanding the principles of organization of these molecules, but just for obtaining structural information on the domain level is emphasized.
Journal ArticleDOI
Structural and physical properties of gelatin extracted from different marine species: a comparative study.
TL;DR: Circular dichroism analysis reveals that gelling involves a refolding of denatured collagen chains into the typical triple helix conformation and, conversely, unfolding upon reheating, and the importance of slow cold maturation is revealed.
Journal ArticleDOI
Procollagen trafficking, processing and fibrillogenesis
TL;DR: Studies of the molecular basis of collagen fibrillogenesis have provided insight into the trafficking of procollagen through the cellular secretory pathway, the conversion of Procollagen to collagen by theprocollagen metalloproteinases, and the directional deposition of fibrils involving the plasma membrane and latesecretory pathway.
Journal ArticleDOI
Characteristics of gelatin from the skins of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus
Soottawat Benjakul,Kwunchit Oungbho,Wonnop Visessanguan,Yaowapa Thiansilakul,Sittiruk Roytrakul +4 more
TL;DR: Gelatins extracted from the skins containing fine scales of two species of bigeye snapper, Priacanthus tayenus (GT), were characterised in this article, where the absorption bands of both gelatins in Fourier transform infrared (FTIR) spectra were mainly situated in the amide band region.
References
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Journal ArticleDOI
The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
TL;DR: The results suggest that hydroxylated proline increases the thermal stability of collagen.
Journal ArticleDOI
Role of pyrrolidine residues in the structure and stabilization of collagen.
John Josse,William F. Harrington +1 more
TL;DR: The physical properties of two neutral salt-soluble invertebrate collagens of markedly different total imino acid and hydroxyproline content have been compared and it is concluded that the total pyrrolidine (Pro + Hypro) rather than the Hypro content alone, is the significant feature in the stabilization of the collagen structure.