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Media type:
E-Article
Title:
Polarized neutron scattering by polarized protons of bovine serum albumin in deuterated solvent
Contributor:
Knop, W.;
Schink, H.-J.;
Stuhrmann, H. B.;
Wagner, R.;
Wenkow-Es-Souni, M.;
Schärpf, O.;
Krumpolc, M.;
Niinikoski, T. O.;
Rieubland, M.;
Rijllart, A.
imprint:
International Union of Crystallography (IUCr), 1989
Description:
<jats:p>Bovine serum albumin (BSA) was dissolved in a mixture of deuterated glycerol and heavy water. The clusters formed by the 3300 proton spins in each BSA molecule were dynamically polarized up to <jats:italic>P</jats:italic> = 40%. Spin-contrast variation in small-angle neutron scattering was studied at several target polarizations. Zero contrast, and hence minimum polarized neutron small-angle scattering, is expected at <jats:italic>P</jats:italic>
<jats:sub>H</jats:sub> = 60% from extrapolation of present data. The three basic scattering functions of spin-contrast variation look very similar because the shape of the BSA molecule and its proton distribution are congruent. Neutron small-angle scattering of BSA is similar to X-ray small-angle scattering at room temperature, indicating no deterioration of the molecular structure of BSA on solidification.</jats:p>