Thermal helix-coil transition in UV irradiated collagen from rat tail tendon.
The thermal helix-coil transition in UV irradiated collagen solution, collagen film and pieces of rat tail tendon (RTT) were compared. Their thermal stability's were determined by differential scanning calorimeter (DSC) and by viscometric measurements. The denaturation temperatures of collagen solution, film and pieces of RTT were different. The helix-coil transition occur near 40 degrees C in collagen solution, near 112 degrees C in collagen film, and near 101 degrees C in pieces of RTT. After UV irradiation the thermal helix-coil transition of collagen samples were changed. These changes depend on the degree of hydratation.
Sionkowska
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Department of Chemistry, N. Copernicus University, Toruñ, Poland.
Kamińska
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D000818:Animals; D002152:Calorimetry, Differential Scanning / Q000379:methods; D003094:Collagen / Q000737:chemistry* / Q000528:radiation effects*; D011487:Protein Conformation; D051381:Rats; D012996:Solutions; D013623:Tail / Q000737:chemistry; D013710:Tendons / Q000737:chemistry*; D014466:Ultraviolet Rays; D014783:Viscosity
D012996:Solutions; D003094:Collagen