Study of the effect of hydration on the dynamics of various globular proteins by Rayleigh scattering of Mössbauer radiation
Kurinov, I.V.; Krupianskiĭ, I.F.; Suzdalev, I.P.; Gol'danskiĭ, V.I.
Biofizika 32(2): 210-214
1987
ISSN/ISBN: 0006-3029 PMID: 3580390 Document Number: 303158
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.