| Literature DB >> 1731902 |
S J Henderson1, P Newsholme, D B Heidorn, R Mitchell, P A Seeger, D A Walsh, J Trewhella.
Abstract
Small-angle X-ray and neutron scattering have been used to characterize the solution structure of rabbit skeletal phosphorylase kinase. The radius of gyration of the unactivated holoenzyme determined from neutron scattering is 94 A, and its maximum dimension is approximately 275-295 A. A planar model has been constructed that is in general agreement with the dimensions of the transmission electron microscope images of negatively stained phosphorylase kinase and that gives values for the radius of gyration, maximum linear dimension, and a pair distribution function for the structure that are consistent with the scattering data.Entities:
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Year: 1992 PMID： 1731902 DOI： 10.1021/bi00117a019
Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162