Collect. Czech. Chem. Commun. 1980, 45, 628-640

Investigation of recrystallization of collagen (I) employing contraction and statistical conformation properties

Antonín Galatík and Anton Blažej

Department of Proteins, Slovak Institute of Technology, 765 82 Otrokovice


The ability of collagen (I) to recrystallize by cooling after a thermal denaturation was attempted by a method of concentration energy and theoretical statistical conformation analysis. Contraction energy of the native collagen was 1.96 ± 0.6 J/g; that of denaturated collagen after cooling in contracted state 0.036 J/g and in the stretched state 0.45 ± 0.1 J/g. This corresponds to a 1.8 and 22.8% of recrystallization, respectively. Theoretic calculation of the probable conformation of the whole sequence of α1(I) chain showed that approximately only 60% of sequences have the ability to form spontaneously stretched polypyrrolidine conformation, whereas approximately 34% of the chain was randomized. About 5% of amino acid sequences had a preferred α-helical conformation and terminal peptides, especially the C-tail have a high probability of extended conformation of a β-pleated sheat type. The collagen chain reveals a significant tendency to form reverse turn. Statistical conformation properties are compared with those of some model polypeptides.