Effects of thermal denaturation on metal binding and ultrastructure in collagen fibrils
β Scribed by J.A. Spadaro; R.O. Becker
- Book ID
- 115749113
- Publisher
- Elsevier Science
- Year
- 1972
- Weight
- 607 KB
- Volume
- 263
- Category
- Article
- ISSN
- 0005-2795
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## Abstract The effects of three glycosaminoglycans (chondroitin 6βsulfate, dermatan sulfate, and hyaluronate) and a proteoglycan on the kinetics of fibril formation and on the thermal stability of the __in vitro__ assembled collagen fibrils, under physiological conditions of ionic strength and pH,
The dependence of the proton spin-lattice relaxation rate, and of the enthalpy and temperature of denaturation on water content, were studied by nmr and differential scanning calorimetry (DSC) in native and denatured collagen. Collagen was first heated at four different temperatures ranging from 40