Isotope-Filtered Affinity NMR

Isotope-Filtered Affinity NMR

A double-editing pulse sequence has been developed that allows the direct observation of protein binding ligand(s) from a mixture of compounds. This technique should aid the discovery of lead pharmaceutical compounds. The proton NMR signals from protein and the nonbinding ligands are simultaneously...

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Veröffentlicht in:Journal of magnetic resonance (1997) 1998-04, Vol.131 (2), p.336-338
Hauptverfasser: Gonnella, Nina, Lin, Mengfen, Shapiro, Michael J., Wareing, James R., Zhang, Xiaolu
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Sprache:eng
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13C isotope editing
affinity NMR
Diffusion NMR
protein binding
pulse sequence
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container_end_page 338
container_issue 2
container_start_page 336
container_title Journal of magnetic resonance (1997)
container_volume 131
creator Gonnella, Nina
Lin, Mengfen
Shapiro, Michael J.
Wareing, James R.
Zhang, Xiaolu
description A double-editing pulse sequence has been developed that allows the direct observation of protein binding ligand(s) from a mixture of compounds. This technique should aid the discovery of lead pharmaceutical compounds. The proton NMR signals from protein and the nonbinding ligands are simultaneously eliminated using13C isotope editing and PFG diffusion-edited NMR. This new experiment is demonstrated using13C/15N-labeled stromelysin catalytic domain (SCD).
doi_str_mv 10.1006/jmre.1997.1376
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language eng
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source Elsevier ScienceDirect Journals
subjects 13C isotope editing
affinity NMR
Diffusion NMR
protein binding
pulse sequence
title Isotope-Filtered Affinity NMR
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