Effect of hydration andpHon the thermal stability of proteinase K
β Scribed by Wang Bangning; Han Buxing; Tan Fu
- Publisher
- Springer Netherlands
- Year
- 1997
- Tongue
- English
- Weight
- 436 KB
- Volume
- 50
- Category
- Article
- ISSN
- 0022-5215
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The endotherm enthalpy changes A H D and temperatures T D of thermal denaturation of tropocollagen fibers were measured by DSC calorinietry as functions of water content. The denaturation temperatures decrease with increasing water content. The enthalpy change values increase sharply in the range 0-
## Abstract Collagen is a triple helical protein, highly hydrated in nature. Bella and Berman (J Mol Biol 1996, 264, 734) have reported the structure of the first hydration layer. Water molecules form bridges of different length around the POG repeats and self assemble into leftβhanded helical wate