title: [Stabilization energy of the compact Caf1(13-149) subunit from Yersinia pestis].
abstract: It has been shown by a variety of methods (circular dichroism, viscosimetry, intrinsic fluorescence, and fluorescence of labels) that, as in the case of small globular proteins the folding-unfolding transition in the Caf1(13-149) subunit under the action of two denaturants (urea and 1,3-dimethylurea) occurs between two major states (unfolded and compact). However, the free energy of the compact structure is only 8/9-9/2 kJ/mol (similar values for single-domain small proteins are in the range of 21-63 kJ/mol).
authors.forename: V M
authors.initials: VM
authors.lastname: Tishchenko
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry*; D013816:Thermodynamics; D015010:Yersinia pestis / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D021122:Protein Subunits; C086725:caf1 protein, Yersinia pestis