Proton nuclear magnetic resonance studies on glutamine-binding protein from Escherichia coli. Formation of intermolecular and intramolecular hydrogen bonds upon ligand binding.

Abstract

Proton nuclear magnetic resonance studies have revealed several structural and dynamic properties of the glutamine-binding protein of Escherichia coli. When this protein binds L-glutamine, six low-field, exchangeable proton resonances appear in the region from +5.5 to +10 parts per million downfield from water (or +10.2 to +14.7 parts per million downfield… (More)

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@article{Shen1989ProtonNM, title={Proton nuclear magnetic resonance studies on glutamine-binding protein from Escherichia coli. Formation of intermolecular and intramolecular hydrogen bonds upon ligand binding.}, author={Qin Cheng Shen and Virgil Simplaceanu and Philippa Cottam and C Kiong Ho}, journal={Journal of molecular biology}, year={1989}, volume={210 4}, pages={849-57} }