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Large‐angle X‐ray diffuse scattering, a new method for investigating changes in the conformation of globular proteins in solutions
Author(s) -
Fedorov B. A.,
Denesyuk A. I.
Publication year - 1978
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/s0021889878013618
Subject(s) - myoglobin , globular protein , scattering , crystallography , small angle x ray scattering , chemistry , molecule , sperm whale , molecular physics , solvent , wide angle x ray scattering , chemical physics , physics , optics , small angle neutron scattering , neutron scattering , organic chemistry
A comparative analysis of the sperm‐whale myoglobin structure in the crystal and in solution has been carried out with the technique previously formulated by the authors which uses the large‐angle X‐ray diffuse scattering for investigating the protein structure in solution. A `modified cube method', correctly taking into account the cavities within the protein molecule accessible to the solvent, is proposed for an accurate estimate of the solvent influence and for calculation of the scattering intensities. A comparison of the theoretical myoglobin scattering curves with the experimental scattering curve of this protein obtained by Stuhrmann shows rather noticeable quantitative divergences, which can be eliminated by a small increase in the distance between the `hairpin' GH and the other part of the protein molecule. It is also shown that several other physically reasonable shifts of helices (or groups of helices) do not lead to an agreement between the experimental and theoretical scattering indicatrices.