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An efficient use of the WATERGATE W5 sequence for observing a ligand binding with a protein receptor
Author(s) -
Furihata Kazuo,
Shimotakahara Sakurako,
Tashiro Mitsuru
Publication year - 2008
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.2264
Subject(s) - chemistry , pulse sequence , sequence (biology) , ligand (biochemistry) , human serum albumin , resonance (particle physics) , nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , receptor , stereochemistry , biochemistry , physics , atomic physics
An efficient pulse sequence for observing a ligand binding with a receptor has been developed by incorporating the WATERGATE W5 sequence. In the conventional water ligand observed via gradient spectroscopy (WaterLOGSY) techniques, the water resonance is selectively excited using,e.g. the double‐pulsed field gradient spin–echo (DPFGSE) sequence at the initial portion of pulse sequence. In the current version, the modified WATERGATE W5 sequence is incorporated at the initial portion of the pulse sequence, and the resonance at the water frequency can be selectively reserved by the modified WATERGATE W5 sequence. The efficiency of ligand‐observed NMR screening techniques has been demonstrated using the human serum albumin (HSA)–tryptophan complex. Copyright © 2008 John Wiley & Sons, Ltd.