RESUMO
The method of tritium planigraphy is used for determination of the accessible surface of a globular protein--lysozyme--and the accessibility of particular types of amino acid residues as a function of temperature in the range of 77-193 K. Protein powder with humidity 10 +/- 1% was used. As the temperature is changed from 77 to 160 K for all types of amino acid residues was obtained decreasing of inclusion of tritium label. All types of amino acid residues may be divided on the three groups: I. Accessibility rises under increasing temperature from 160 to 293 K (K, R, H, P, L); II. Accessibility not depends or slightly increases with the growth of temperature (C, V, A, I, Y, F); III. Accessibility strongly increases in the range of the temperature 260-293 K (S, T, G, D + N, E + Q). The reason of "cold denaturation" is perhaps the difference of behaviour of structural water molecules. Under increasing of temperature from 160 to 293 K change of accessibility was explained the growing of intramolecular flexibility of molecule. Under transition from 160 to 77 K for all types of residues is observed sensible change of spatial structure of the protein, which cannot be explained by only participation of dynamical characteristics.
