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 | |
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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. |
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AbstractList | 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 angstrom, and its maximum dimension is approximately 275-295 angstrom. 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. 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 {angstrom}, and its maximum dimension is approximately 275-295 {angstrom}. 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. |
Author | Mitchell, R Walsh, D. A Newsholme, P Trewhella, J Heidorn, D. B Henderson, S. J Seeger, P. A |
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Keywords | Vertebrata Mammalia Neutron scattering Enzyme Rabbit X ray scattering Lagomorpha Striated muscle Phosphorylase kinase Structural analysis |
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Snippet | Small-angle X-ray and neutron scattering have been used to characterize the solution structure of rabbit skeletal phosphorylase kinase. The radius of gyration... |
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SubjectTerms | 550600 - Medicine Analytical, structural and metabolic biochemistry ANIMALS AQUEOUS SOLUTIONS Biological and medical sciences DISPERSIONS Enzyme Activation ENZYMES Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology GEOMETRY MAMMALS MATHEMATICS MIXTURES Models, Molecular MOLECULAR STRUCTURE neutron scattering Neutrons ORGANIC COMPOUNDS PHOSPHORUS-GROUP TRANSFERASES phosphorylase kinase Phosphorylase Kinase - chemistry Phosphorylase Kinase - radiation effects PHOSPHOTRANSFERASES PROTEINS RABBITS RADIOLOGY AND NUCLEAR MEDICINE SCATTERING Scattering, Radiation skeletal muscle SOLUTIONS structure Structure-Activity Relationship TRANSFERASES VERTEBRATES X-Ray Diffraction |
Title | Solution structure of phosphorylase kinase studied using small-angle x-ray and neutron scattering |
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