Biopolymers and cell. 1990. Volume 6. № 4. 84 - 91

A. S. Ladokhin

EQUILIBRIUM DYNAMICS OF PROTEIN. STUDIES IN PROPER FLUORESCENCE OF MELITTIN

Summary

    Structural-dynamic organization of melittin molecule has been studied in detail within a wide temperature range. Spectral changes of proper fluorescence for tetra-dimensional milittin observed at low temperatures depend on dissociation rather than on variations in mobility of dipoles as at high temperatures. The previously obtained values of para¬meters for dipolc-orienation mobility of tryptophanyl surroundings are refined. It is shown that value of activation energy of equilibrium structural fluctuations in tetra-dimensional melittin permitting both external quenching agent and quenching groups of protein itself to interact with tryptophanyl equals 10-15 kJ/mol. Reorientation activation energy of internal dipole melittin groups is 30 kJ/mol.