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Ramstein, J ; Locker, D ; Bianchi, ME ; Leng, M
Domain-domain interactions in high mobility group 1 protein (HMG1)
European Journal of Biochemistry 260 (3) 692-700
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Abstract :
The high mobility group protein HMG1 is a conserved chromosomal protein with two homologous DNA-binding domains, A and B, and an acidic carboxy-terminal tail, C. The structure of isolated domains A and B has been previously determined by NMR, but the interactions of the different domains within the complete protein were unknown. By means of differential scanning calorimetry and circular dichroism we have investigated the thermal stability of HMG1, of the truncated protein A-B (HMG1 without the acidic tail C) and of the isolated domains A and B. In 3 mM sodium acetate buffer, pH 5, the thermal melting of domains A and B are identical (transition temperature t(m) = 43 degrees C and 41 degrees C, denaturation enthalpies Delta H = 46 kcal.mol(-1)).