Thermodynamic and hydrodynamic study of Bence-Jones proteins

Autor:	V. S. Khristoforov, O. P. Bliznyukov, V. M. Tishchenko
Rok vydání:	2009
Předmět:	Circular dichroism Structural Biology Chemistry Phosphate buffered saline Biophysics Complete protein Analytical Centrifugation Amyloid fibril Constant (mathematics) Fluorescence Bence Jones protein
Zdroj:	Molecular Biology. 43:134-141
ISSN:	1608-3245 0026-8933
DOI:	10.1134/s002689330901018x
Popis:	Four Bence-Jones proteins were studied under physiological conditions (10 mM phosphate buffer solution (pH 7.0) and 100 mM NaCl) by the circular dichroism, fluorescence, and analytical centrifugation methods. Combined analysis of the optical melting curves for the proteins and their fragments demonstrated that the stability of VAD protein and its constant half was decreased as compared with the other Bence-Jones proteins. This was correlated with the ability of both the whole protein and its constant (but not variable) part to form amyloid fibrils. The data on the correlation of the decreased stability with an abnormal interaction of two constant CL domains are reported.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::d32a188287209b64f03384b8bf1f8771 https://doi.org/10.1134/s002689330901018x Zobrazit plný text záznamu Full text from SpringerLink