𝔖 Bobbio Scriptorium
✦   LIBER   ✦

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

No coin nor oath required. For personal study only.


📜 SIMILAR VOLUMES


X-ray crystallographic studies of the de
✍ Girish S Ratnaparkhi; R Varadarajan 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 323 KB 👁 2 views

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

A study of the thermal denaturation of r
✍ David R. Goodlett; Rachel R. Ogorzalek Loo; Joseph A. Loo; Jon H. Wahl; Harold R 📂 Article 📅 1994 🏛 Elsevier Science 🌐 English ⚖ 894 KB

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