[A study of the effect of solvent composition and viscosity on the molecular dynamics of human serum albumin using Rayleigh scattering of Mössbauer radiation].
By means of RSMR changes of human serum albumen intramolecular mobility by addition of 1.5% and 7.5% of glutar dialdehyde (GD) in concentrated protein solution, heat denaturation of a protein or substitution of water by water-glycerol solvent with amount of water to glycerol: 1 to 2 were studied. It is shown that the elastic fraction for HSA is changed much less addition of GD or by heat denaturation than by substitution of water solution by water-glycerol. It seems that the observed strong influence of glycerol on intramolecular mobility of HSA is connected mostly with effective dehydration of protein (by substitution of the part of a water solvent by glycerol) and with a small volume decrease of protein (due to preference hydration effect) rather than with the increase of the solvent viscosity.
Kurinov
I V
IV
Krupianskiĭ
Iu F
IuF
Genkin
M V
MV
Davydov
R M
RM
Suzdalev
I P
IP
D006801:Humans; D008027:Light; D008433:Mathematics; D012542:Scattering, Radiation; D012709:Serum Albumin / Q000032:analysis*; D012997:Solvents / Q000032:analysis*; D013057:Spectrum Analysis; D014783:Viscosity
D012709:Serum Albumin; D012997:Solvents
Izuchenie vliianiia sostava i viazkosti rastvoritelia na molekuliarnuiu dinamiku syvorotochnogo al'bumina cheloveka metodom releevskogo rasseianiia messbauérovskogo izlucheniia.