Journal ArticleDOI
A hypothesis on the role of hydroxyproline in stabilizing collagen structure.
TLDR
It is proposed that, in addition to stabilizing the collagen triple-helical structure due to the stereochemical properties of the pyrrolidine ring, hydroxyproline gives added stability by the formation of an extra hydrogen bond.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 1973-09-21. It has received 182 citations till now. The article focuses on the topics: Collagen helix & Hydrogen bond.read more
Citations
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Book ChapterDOI
Turns in peptides and proteins.
TL;DR: The aim of this chapter is to examine structural and functional roles of turns in peptides and proteins.
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
Hydration structure of a collagen peptide.
TL;DR: The roles of hydroxyproline and hydration are strongly interrelated in the structure of the collagen triple helix and the extensively ordered hydration structure offers a good model for the interpretation of the experimental results on collagen stability and assembly.
Book ChapterDOI
Molecular structure of the collagen triple helix.
TL;DR: High-resolution crystal structures obtained for collagen model peptides confirm the supercoiled triple helix conformation, and provide new information on hydrogen bonding patterns, hydration, sidechain interactions, and ligand binding.
Journal ArticleDOI
Reverse turns in peptides and proteins.
TL;DR: In this article, reverse turns in Peptides and Protein are discussed and discussed in the context of protein synthesis and protein protein synthesis, and a review of the review is given, with a focus on protein synthesis.
References
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Book ChapterDOI
Conformation of Polypeptides and Proteins
TL;DR: This chapter considers the parameters that are required for an adequate description of a polypeptide chain and the mathematical method of utilizing these parameters for calculating the coordinates of all the atoms in a suitable frame of reference so that all the interatomic distances, and bond angles, can be calculated and their consequences worked out.
Journal ArticleDOI
Structure of Collagen
TL;DR: It has been found that it is possible to build up a two-bonded structure (two hydrogen bonds for three residues) while retaining all contacts within permissible values, and the actual parameters of the minor helix of the collagen structure have been re-determined.
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.
Book ChapterDOI
The structure of collagen and gelatin.
Harrington Wf,Von Hippel Ph +1 more
TL;DR: This chapter reviews that collagen constitutes the major protein component of skin, bone, tendon, and all the other forms of connective tissue and that the collagen ⇆ gelatin transformation in solution has been recognized as a reversible first-order phase transition, subject to the same physical laws which govern the crystalline ⇆ amorphous phase transitions observed in systems of linear polymers.