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Organization of turnip yellow mosaic virus investigated by neutron small angle scattering at 80 K: An intermediate state preceding decapsidation of the virion?
Author(s) -
Witz Jean,
Timmins Peter A.,
Adrian Marc
Publication year - 1993
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340170302
Subject(s) - capsid , neutron scattering , radius , rna , neutron , crystallography , scattering , turnip yellow mosaic virus , chemistry , virus , physics , molecular physics , virology , biology , optics , nuclear physics , biochemistry , gene , computer security , computer science
The organization of turnip yellow mosaic virus has been investigated by neutron small angle scattering at 300 K and 80 K in buffers containing various amounts of D 2 O. We confirm that in native virions, no substantial part of the RNA is located at a radius larger than ca. 100‐110 Å, i.e., that there is very little interpretation of the RNA into the capsid. At 80 K, scattering curves do not depend much upon contrast, from 40% D 2 O to 100% D 2 O buffers, but are strongly affected by interparticle interference. We could, however, show that it is not the case for the subsidiary intensity maximum at q ∼ 0.06 Å −1 . From the position of this maximum, we conclude that upon freezing, the radius of the capsid expands by c.a. 3.5% and the RNA penetrates deeply into the protein shell. Biological implications of this conformational change immediately preceding decapsidation are dicussed. © 1993 Wiley‐Liss, Inc.