Nuclear magnetic resonance study of the complexes of manganese(II) and fully adenylated glutamine synthetase (Escherichia coli W). Frequency, temperature, and substrate dependence of water proton relaxation rates.
作者信息
Villafranca J J, Wedler F C
出版信息
Biochemistry. 1974 Jul 30;13(16):3286-91. doi: 10.1021/bi00713a017.
PMID:4152181
Abstract
摘要
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Nuclear magnetic resonance study of the complexes of manganese(II) and fully adenylated glutamine synthetase (Escherichia coli W). Frequency, temperature, and substrate dependence of water proton relaxation rates.
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Topographical analysis of regulatory and metal ion binding sites on glutamine synthetase from Escherichia coli: 13C and 31P nuclear magnetic resonance and fluorescence energy transfer study.
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