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Determination of Amide Proton CSA in15N-Labeled Proteins Using1H CSA/15N–1H Dipolar and15N CSA/15N–1H Dipolar Cross-Correlation Rates

✍ Scribed by Marco Tessari; Frans A.A Mulder; Rolf Boelens; Geerten W Vuister

Publisher
Elsevier Science
Year
1997
Tongue
English
Weight
156 KB
Volume
127
Category
Article
ISSN
1090-7807

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✦ Synopsis

Knowledge of the magnitude and orientation of the am-is set up as a constant-time experiment in which the reference experiment is ( virtually ) free of 15 N CSA / DD relax-ide-proton chemical shift anisotropy ( CSA ) is of great interest because of its correlation with hydrogen bonding and ation interference effects.

At time point a in the sequence, antiphase 15 N magneti-secondary structure (1) . Information about the CSA of amide protons can be obtained from solid-state NMR measure-zation, 2I z S y , has been created where I and S denote the 1 H N and 15 N spin operators of the product-operator for-ments, but so far only a few experimental observations have been reported limited to small synthetic 15 N-labeled peptides malism ( 14) , respectively. In the presence of 15 N CSA/ DD cross-correlation the antiphase 15 N magnetization and organic molecules (2-5). An alternative approach employs the measurement of cross-correlation effects in solu-will be partially converted to in-phase 15 N magnetization ( 8, 10, 11, 13 ) so that at time point b the following terms tion between the amide-proton CSA and amide-proton-15 N dipolar interactions ( 1 H N CSA/DD). The CSA/ DD cross are generated: correlation contains information on the motional properties and the anisotropy of the chemical shift tensor (6)(7)(8)(9)(10)(11)(12).

2I z S y

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