[Number of hydrogen bonds in the structure of collagen]

The kinetics of hydrogen exchange of collagens from different animals was studied by the radioisotopic method (tritium) and infrared spectroscopy (deuterium). It has been shown that collagens from different animals (rat, pike, cod, carp, frogs) differ in amino acid composition and thermostability but are similar in the amount of slowly exchanged hydrogens. All the studied collagens have (1.00 +/- 0.05) very slowly exchanged hydrogens per triplet and (0.6 +/- 0.1) slowly exchanged hydrogens per triplet. Identifying the quantity of slowly exchanged hydrogens with the quantity of hydrogen bonds in the macromolecule, it can be concluded that collagens differing in stability do not differ by the quantity and composition of intramolecular hydrogen bonds.