[Enthalpic denaturation of collagen satisfies the general relation of the change in Delta H(d) from Delta C(p) for proteins at zero hydroxyproline level].
One of the noticeable peculiarities of thermodynamics of collagen is an anomalous high magnitude of the enthalpy of denaturation delta Hd at a very low thermostability. Taking into account recent ideas about the role of hydrophobic interactions in determination of the thermodynamic function of protein denaturation, it is shown that the high magnitude of delta Hd of collagen in comparison with those of globular proteins can be explained by two factors: a significant contribution of residues of 4-hydroxyproline and small magnitude of hydrophobic interactions.
Burdzhanadze
T V
TV
Natishvili Institute of Experimental Morphology, Academy of Sciences of Georgia, Tbilisi, Georgia.
D003094:Collagen / Q000737:chemistry*; D006909:Hydroxyproline / Q000032:analysis*; D011489:Protein Denaturation; D013816:Thermodynamics
D003094:Collagen; D006909:Hydroxyproline
Ental'piia denaturatsii kollagena udovletvoriaet obshcheĭ zakonomernosti izmeneniia Delta H(d) ot Delta C(p) dlia belkov pri nulevom soderzhanii oksiprolina.