[Study of the effect of hydration on the dynamics of various globular proteins by Rayleigh scattering of Mössbauer radiation].
Hydration relationships of the elastic scattering fraction of Mössbauer radiation were studied for human serum albumin (HSA), pancreatic trypsin inhibitor and lysozyme within hydration degrees 0 less than or equal to h less than or equal to 0.75 g/g (at T = 295 degrees K) and temperatures 100K less than or equal to T less than or equal to 320 K (for HSA only at h = 0.03; 0.25; 0.41; 0.65). It is shown that the increase of both hydration degree above h greater than 0.1 and temperature above T greater than 200K leads to the appearance of intramolecular mobility in these proteins.
D006801:Humans; D011487:Protein Conformation; D011506:Proteins; D012542:Scattering, Radiation; D013057:Spectrum Analysis; D014867:Water
D011506:Proteins; D014867:Water
Izuchenie vliianiia gidratatsii na dinamiku nekotorykh globuliarnykh belkov metodom réleevskogo rasseianiia messbauérovskogo izlucheniia.