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Vol 45(2011) N 6 p. 967-975;
V.M. Tishchenko*

Effects of Interdomain Interactions on Amyloidogenic Properties of Bence Jones Proteins

Institute of Biological Instrumentation Russian Academy of Science, Pushchino, Moscow Region, Pushchino, 142290 Russia

*tischen@vega.protres.ru
Received - 2010-12-31; Accepted - 2011-03-30

Isolated constant domains of two Bence Jones proteins, VAD and BIR, are able to form amyloid fibrils, but only the first one retains this feature within the intact protein. The conformation and stability of these proteins were studied using scanning microcalorimetry, circular dichroism, fluorescence spectroscopy, and analytical centrifugation at physiological conditions (10 mM phosphate buffer, pH 7.0, 100 mM NaCl), and it was shown that isolated pairs of constant domains (СL-CL) of VAD and BIR had reduced stability in comparison to ordinary (nonamyloidogenic) Bence Jones proteins. However, in the intact BIR protein, the stability of the constant domain block increased dramatically, in agreement with the loss of ability to form amyloid fibrils.

Bence-Jones proteins, amyloid fibrils, constant domain, stability, СL-CL intеr-domain interaction



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