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Default Closed form of liganded glutamine-binding protein by rotational-echo double-resonance

Closed form of liganded glutamine-binding protein by rotational-echo double-resonance NMR.

Related Articles Closed form of liganded glutamine-binding protein by rotational-echo double-resonance NMR.

Biochemistry. 1997 Aug 5;36(31):9405-8

Authors: Klug CA, Tasaki K, Tjandra N, Ho C, Schaefer J

Rotational-echo double-resonance NMR has been used to determine internuclear distances in the complex of glutamine-binding protein and its ligand, l-glutamine. The distances between the ligand and Tyr185 are consistent with the results of molecular dynamics simulations constrained by three REDOR-determined distances to His156. This model is also consistent with six other REDOR-determined internuclear distances, most of which agree with values from the first report of an X-ray structure of the complex of glutamine-binding protein and l-glutamine.

PMID: 9235984 [PubMed - indexed for MEDLINE]



Source: PubMed
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