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Vol 43(2009) N 1 p. 134-141; V.M. Tishchenko1, V.S. Khristoforov2, O.P. Bliznyukov3 Thermodynamic and hydrodynamic study of Bence-Jones proteins 1Institute of Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290, Russia2Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290, Russia 3Institute of Immunology, Ministry of Public Health of the Russian Federation, Moscow, 115478, Russia Received - 2008-04-16; Accepted - 2008-06-06 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 CLdomains are reported. Bence-Jones proteins, amyloid fibrils, constant domains, stability, CL-CL interdomain interaction |
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