Thermodynamic stability of ribonuclease A at 25 degrees C in aqueous solutions of guanidine hydrochloride, urea and alkylureas

Authors
Poklar, N Lah, N Oblak, M Vesnaver, G
Citation
N. Poklar et al., Thermodynamic stability of ribonuclease A at 25 degrees C in aqueous solutions of guanidine hydrochloride, urea and alkylureas, ACTA CHIM S, 46(3), 1999, pp. 315-322
Citations number
20
Categorie Soggetti
Chemistry
Journal title
ACTA CHIMICA SLOVENICA
ISSN journal
13180207 → ACNP
Volume
46
Issue
3
Year of publication
1999
Pages
315 - 322
Database
ISI
SICI code
1318-0207(1999)46:3<315:TSORAA>2.0.ZU;2-0
Abstract
The previously published results of the effect of pH, guanidinium hydrochlo ride (GuHCl), urea, methylurea, N,N'-dimethylurea, ethylurea and butylurea on the thermal stability of ribonuclease A (RNase A) studied by differentia l scanning calorimetry (DSC) (N. Poklar, N. Petroveie, M. Oblak, G. Vesnave r, Protein Sci. 1999, 8, 832-840) were used to calculate the RNase A thermo dynamic stability at 25 degrees C. It has been shown that thermodynamic sta bility of RNase A at 25 degrees C decreases with increasing concentration o f denaturants and the size of the hydrophobic group substituted on the urea molecule.