An analysis of chemistries known to confer high hydrothermal stability to collagen has arrived at a series of conditions that must be met. These include the formation of a stable supramolecular matrix, which must be firmly bound to the collagen triple helices. In most stabilising reactions, the chemical reactions are limited to linking elements of the collagen structure to a relatively unstable matrix. Typically, this linking step confers only moderate hydrothermal stability because the matrix is readily displaced by shrinking. In those chemical processes which result in high hydrothermal stability, the linking step is combined with an additional step that locks the components of the matrix together. In this way, the matrix acts like a sing...
The folding of triple-helical collagen, the most abundant protein in nature, relies on the nucleatio...
AbstractCollagen molecules in solution unfold close to the maximum body temperature of the species o...
Differential scanning calorimetry (DSC) was used to study the thermal stability of native and synthe...
Type I collagen is the most common protein among higher vertebrates. It forms the basis of fibrous c...
BACKGROUND: Type I collagen is the most common protein among higher vertebrates. It forms the basis ...
Mineralised collagen displays an improved hydrothermal stability compared to collagen that is unmine...
The molecular structure of collagen is now accepted to be based on a triple-stranded coiled-coil, in...
AbstractThe mechanism that renders collagen molecules more stable when precipitated as fibers than t...
UNLABELLED: We provide evidence to show that the standard reactant concentrations used in tissue eng...
The possibility of hydroxyproline residues stabilizing the collagen triple-helical structure by the ...
Stabilization of type I rat tail tendon (RTT) collagen by various aldehydes, viz. formaldehyde, glut...
The thermal stability of the trimeric species formed by seven type I collagen CNBr peptides was dete...
The analysis of factors contributing to the stability of proteins is a subject of intense debate. Pa...
Trans amide bonds and fast cis–trans isomerization of Xaa-Pro bonds are crucial for the stability an...
This study aims to characterize and understand the effects of freezing on collagen structures and fu...
The folding of triple-helical collagen, the most abundant protein in nature, relies on the nucleatio...
AbstractCollagen molecules in solution unfold close to the maximum body temperature of the species o...
Differential scanning calorimetry (DSC) was used to study the thermal stability of native and synthe...
Type I collagen is the most common protein among higher vertebrates. It forms the basis of fibrous c...
BACKGROUND: Type I collagen is the most common protein among higher vertebrates. It forms the basis ...
Mineralised collagen displays an improved hydrothermal stability compared to collagen that is unmine...
The molecular structure of collagen is now accepted to be based on a triple-stranded coiled-coil, in...
AbstractThe mechanism that renders collagen molecules more stable when precipitated as fibers than t...
UNLABELLED: We provide evidence to show that the standard reactant concentrations used in tissue eng...
The possibility of hydroxyproline residues stabilizing the collagen triple-helical structure by the ...
Stabilization of type I rat tail tendon (RTT) collagen by various aldehydes, viz. formaldehyde, glut...
The thermal stability of the trimeric species formed by seven type I collagen CNBr peptides was dete...
The analysis of factors contributing to the stability of proteins is a subject of intense debate. Pa...
Trans amide bonds and fast cis–trans isomerization of Xaa-Pro bonds are crucial for the stability an...
This study aims to characterize and understand the effects of freezing on collagen structures and fu...
The folding of triple-helical collagen, the most abundant protein in nature, relies on the nucleatio...
AbstractCollagen molecules in solution unfold close to the maximum body temperature of the species o...
Differential scanning calorimetry (DSC) was used to study the thermal stability of native and synthe...