Temperature-Induced Denaturation of Ribonuclease S: A Thermodynamic Study †
✍ Scribed by Catanzano, Francesca; Giancola, Concetta; Graziano, Giuseppe; Barone, Guido
- Book ID
- 126977474
- Publisher
- American Chemical Society
- Year
- 1996
- Tongue
- English
- Weight
- 319 KB
- Volume
- 35
- Category
- Article
- ISSN
- 0006-2960
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In an attempt to view the onset of urea denaturation in ribonuclease we have collected X-ray diffraction data on ribonuclease S crystals soaked in 0, 1.5, 2, 3, and 5 molar urea. At concentrations above 2 M urea, crystals were stabilized by glutaraldehyde crosslinking. We have also collected data on
The thermal stability of ribonuclease S (RNase S), an enzymatically active noncovalent complex composed of a 2166-u peptide (S-peptide) and a 11,534-u protein (S-protein), was investigated by electrospray ionization mass spectrometry (ESI-MS) and capillary electrophoresis ESI-MS (CE-ESI-MS). The int