[Self-assembly of collagen type I molecules without telopeptides].
The effect of temperature on the kinetics of formation of fibrils from rat tail collagen molecules devoid of telopeptides was studied. It was shown that the rats of fibril formation at 30 and 35 degrees C increases five- and eightfold, respectively, as compared with that at 25 degrees C. It was found that enthalpy of fibril denaturation at 30 degrees C is maximal for the collagen both with intact telopeptides and devoid of telopeptides. It was found that essential for the fibrilogenesis of type I collagen devoid of telopeptides are temperatures of 30 and 35 degrees C.
Nikolaeva
T I
TI
Pisachenko
A I
AI
Selezneva
I I
II
Rochev
Iu A
IuA
Gavriliuk
B K
BK
D000818:Animals; D003094:Collagen / Q000737:chemistry*; D007700:Kinetics; D011489:Protein Denaturation; D051381:Rats; D013696:Temperature; D013816:Thermodynamics
D003094:Collagen