Solution structure of phosphorylase kinase studied using small-angle x-ray and neutron scattering
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 mode...
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Published in | Biochemistry (Easton) Vol. 31; no. 2; pp. 437 - 442 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Chemical Society
21.01.1992
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Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | istex:6CE0ADEB2FC7257A4506DCF9AE9C4A61EEA0B48D ark:/67375/TPS-XFHD9K2V-R ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 W-7405-ENG-36 |
ISSN: | 0006-2960 1520-4995 |
DOI: | 10.1021/bi00117a019 |