THERMODYNAMICS OF PROTEIN STABILITY - A FAMILY OF RIBONUCLEASES

Citation
G. Barone et al., THERMODYNAMICS OF PROTEIN STABILITY - A FAMILY OF RIBONUCLEASES, Pure and applied chemistry, 69(11), 1997, pp. 2307-2313
Citations number
44
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry
Journal title
ISSN journal
0033-4545
Volume
69
Issue
11
Year of publication
1997
Pages
2307 - 2313
Database
ISI
SICI code
0033-4545(1997)69:11<2307:TOPS-A>2.0.ZU;2-6
Abstract
Ribonucleases constitute a ubiquitous superfamily of enzymes. Besides the well known hydrolytic activity against the RNAs, recently some of the proteins of this group, the so called RISBASE, have shown to posse ss a multiplicity of biological functions. In this article a short rev iew is reported concerning systematic thermodynamic studies carried ou t at our laboratory mainly by means of differential scanning calorimet ry on the well known ribonuclease A, RNase A, and its congeners. Among them, dimeric natural ribonuclease, BS-RNase, extracted from bull sem inal plasma or vesicles, has shown very interesting features.