title: [The influence of interdomain interaction on the amyloidogenic properties Bence-Jones proteins].
abstract: Isolated constant domains from two Bence-Jones proteins VAD and BIR able to form amyloid fibrils, whereas only the first of them to keep specific ability of the intact protein. Studies of conformation and stability of these proteins by scanning microcalorimetry, circular dichroism, fluorescence and analytical centrifugation at physiological conditions (10 mM phosphate buffer, pH 7.0, 100 mM NaCl) showed that the stability of isolated pair of constant domains (C(L)-C(L)) VAD and BIR is reduced by compared with standard (nonamyloidogenic) Bence-Jones protein. However, in the intact protein BIR stability of his constant domains increases sharply, which correlated with the loss of the protein ability to form amyloid fibrils.
authors.forename: V M
authors.initials: VM
authors.lastname: Tishchenko
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D058227:Amyloidogenic Proteins / Q000737:chemistry*; D001536:Bence Jones Protein / Q000737:chemistry*; D002151:Calorimetry; D002498:Centrifugation; D002942:Circular Dichroism; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry*; D055550:Protein Stability; D017434:Protein Structure, Tertiary
chemical_list: D000682:Amyloid; D058227:Amyloidogenic Proteins; D010446:Peptide Fragments; D001536:Bence Jones Protein