Related Experiment Video
Updated: Aug 18, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
Published on: September 20, 2012
Stability of collagen during denaturation
R Penkova1, I Goshev, S Gorinstein
1Department of Chemistry and Biochemistry, Medical University, Pleven, Bulgaria.
Abstract:
The stability of calf skin collagen (CSC) type I during thermal and chemical denaturation in the presence of glycerol was investigated. Thermal denaturation of type I collagen was performed in the presence of glycerol or in combination with urea and sodium chloride. The denaturation curves obtained in the presence of urea or sodium chloride retained their original shape without glycerol. These curves were shifted upward proportionally to the glycerol concentration in the reaction medium. This means that glycerol and the denaturants act independently. The explanation is based on the difference in the mechanism of their action on the collagen molecule.
Related Concept Videos
Protein Folding
Structural Protein Function
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Collagens are the Major Structural Proteins of ECM
Connective tissue proper includes loose...
Type IV Collagen of Basal Lamina
A type IV collagen molecule has six alpha chains which can exist in...
Protein Denaturation

