[Effects of glassing in aqueous protein systems].
Explore the source record for details and available documents.
Biomedical subjects
Publications and source records attributed to V I Gol'danskiĭ.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
The measurements of angle dependencies of total and elastic Rayleigh scattering of Mossbauer radiation intensities have been performed for human serum albumin (HSA) with hydration degrees h = 0.13 and h = 0.4. The extended model was developed for calculating the inelastic intensity of Rayleigh scattering. Original data for HSA and published data on met-Mb were fitted within the frame of this model. The best agreement with experiment was obtained when two types of intraglobular motions were taken into account: individual motions of small side-chain groups and cooperative (mechanical) motions of segments (most probable alpha-helices). Long-range correlated motions are essential at low hydration degree. The possibilities of application of the coherent version of RSMS technique are described.
The possibility of using gamma resonance spectroscopy (GRS) for studying the dynamics of water-protein systems is shown in the present work. The experiments were carried out on an albumin-water system. The results obtained are compared with those obtained by the spin label method under the same conditions. The different behaviour of Fe ions which are firmly- and weakly-related with the protein matrix allows to separate the mobility of the whole protein macromolecule and also the mobility of its subunits.