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July 1, 1974Biochemistry

Nuclear magnetic resonance study of the complexes of manganese(II) and fully adenylylated glutamine synthetase (Escherichia coli W). Frequency, temperature, and substrate dependence of water proton relaxation rates

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JVJoseph J. VillafrancaFWF. C. Wedler

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Villafranca et al. (1974) studied this question.

synapsesocial.com/papers/6a99069db0871bb756e113bfhttps://doi.org/10.1021/bi00713a017
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1The Regulation of Glutamine Synthesis in Microorganisms1970 · 192 citations
  2. 2Calorimetric study of the interaction of Mn<sup>2+</sup> with glutamine synthetase from Escherichia coli1972 · 27 citations
  3. 3Conformational changes in glutamine synthetase from Escherichia coli. I. Binding of manganese ion in relation to some aspects of the enzyme structure and activity1969 · 72 citations
  4. 45′-Adenylyl-O-tyrosine1968 · 177 citations
  5. 5The Activated Complex and the Absolute Rate of Chemical Reactions.1935 · 1,027 citations