Collagen folding

The principles of collagen folding differ markedly from other known proteins since single monomers cannot fold. Triple helix folding is a multi-step process involving chain association, registration, nucleation and... 

Catalysts of Collagen Folding, Co- and Post-Translational Modification... 

H. P. Bachinger J. Engel, The Thermodynamics and Kinetics of Collagen Folding. In Protein Folding Handbook J. Buchner,... 

Perret, S., Merle, C., Bernocco, S., Berland, P., Garrone, R., Hulmes, D.J., Theisen, M., and Ruggiero, F. (2001). Unhydroxylated triple helical collagen I produced in transgenic plants provides new clues on the role of hydroxyproline in collagen folding and fibril formation. J. Biol. Chem. 276, 43693-43698. 

Bachinger HP, Engel J. The thermodynamics and kinetics of collagen folding. In lYotein Folding Handbook. Buchner J, Kiefhaber T, eds. 2005. Wiley, New York. 

Recent comparative studies on the rate of formation of the collagen-fold in HjO and DsO seem to support the possibility of intrachain water bridges linking adjacent carbonyl oxygens. These studies are discussed in Section V. 

Kinetics of Optical Rotatory Changes During the Oelatin Collagen-Fold Transition... 

Rate of Formation of the Collagen-Fold in Different Gelatins, Following Quenching to 3.7°C... 

The formation of the unique collagen-fold type structure along individual chains makes possible lateral chain association, which may be monitored by the relatively slow changes in viscosity and light scattering accompanying this step. 

Collagen. Bensusan and Nielsen (1964) have obtained information on the mechanism of the gelatin - collagen-fold transition by a direct experimental approach of determining the rate of formation of hydrogen bonds between peptide... 

At very low concentrations (<0.1%) intramolecular bonds are formed preferentially by back folding of the single chains. At concentrations above 1% the helix growth induces chain association and three-dimensional network formation. For that purpose two subsequent processes are involved a) the formation of single helix nuclei and b) aggr ation of these single helices to a triple helix. It appears that the extent and manner of reversion to the collagen fold (triple helix) structure is dq)endent on solvent, temperature and concentration. 

A similar phenomenon can be observed when a polymer gel is placed in a container and swollen. Tanaka et al. analyzed this phenomenon using linear stability analysis [13]. For a gelatin gel, Amiya et al. reported that the same behavior as the other gels could be observed [14]. However, when the corresponding behavior on the photosensitive material was investigated, it behaved quahtatively similarly but its magnitude was smaller. It was hypothesized that this is due to the coexistence of collagen folds and crosslink structure. 

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