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The Allosteric activator Mg-ATP Modifies the Quaternary Structure of the R-state of Escherichia coli Aspartate Transcarbamylase Without Altering the T↔R Equilibrium

✍ Scribed by L. Fetler; P. Vachette


Book ID
115631051
Publisher
Elsevier Science
Year
2001
Tongue
English
Weight
624 KB
Volume
309
Category
Article
ISSN
0022-2836

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Solution scattering curves evaluated from the crystal structures of the T and R states of the allosteric enzyme aspartate transcarbamylase from Escherichia coli were compared with the experimental x-ray scattering patterns. Whereas the scattering from the crystal structure of the T state agrees with