Stability and folding studies of two homologous proteins, human stefins A and B

Citation
E. Zerovnik et al., Stability and folding studies of two homologous proteins, human stefins A and B, ACTA CHIM S, 45(2), 1998, pp. 161-171
Citations number
44
Categorie Soggetti
Chemistry
Journal title
ACTA CHIMICA SLOVENICA
ISSN journal
13180207 → ACNP
Volume
45
Issue
2
Year of publication
1998
Pages
161 - 171
Database
ISI
SICI code
1318-0207(1998)45:2<161:SAFSOT>2.0.ZU;2-N
Abstract
In a shorter Introduction we describe the usual experimental means of how t o study protein stability and folding. Our work on stability of human stefi ns A and B, determined by chemical, heat, and pH denaturation, is described next. We explain the folding mechanism of human stefin B (as determined th us far) and compare it to homologous human stefin A, in particular, the dep endence of folding rates on the concentration of GuHCl. pH denaturation of human stefin B (E.Zerovnik et al., Eur. J. Biochem. 1997, 245, 364-372) and its folding to the native state are described in more detail.