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Polarized neutron scattering by polarized protons of bovine serum albumin in deuterated solvent
Author(s) -
Knop W.,
Schink H.J.,
Stuhrmann H. B.,
Wagner R.,
WenkowEsSouni M.,
Schärpf O.,
Krumpolc M.,
Niinikoski T. O.,
Rieubland M.,
Rijllart A.
Publication year - 1989
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889889004073
Subject(s) - bovine serum albumin , deuterium , small angle neutron scattering , scattering , neutron scattering , biological small angle scattering , neutron , spins , chemistry , proton spin crisis , small angle scattering , proton , neutron diffraction , small angle x ray scattering , molecule , molecular physics , analytical chemistry (journal) , crystallography , nuclear magnetic resonance , atomic physics , optics , physics , nuclear physics , chromatography , crystal structure , condensed matter physics , organic chemistry
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 P = 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 P H = 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.