1H– 13C separated local field spectroscopy of uniformly 13C labeled peptides and proteins

By incorporating homonuclear decoupling on both the 1H and 13C channels it is feasible to obtain high-resolution two-dimensional separated local field spectra of peptides and proteins that are 100% labeled with 13C. Dual-PISEMO (Polarization Inversion Spin Exchange Modulated Observation) can be perf...

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Bibliographic Details
Published in:Journal of magnetic resonance (1997) 2010-09, Vol.206 (1), p.105-111
Main Authors: Lin, Eugene C., Wu, Chin H., Yang, Yuan, Grant, Christopher V., Opella, Stanley J.
Format: Article
Language:English
Subjects:
13C NMR
Bacteriophages - chemistry
Carbon Radioisotopes - chemistry
Electromagnetic Fields
Hydrogen - chemistry
Indicators and Reagents
Isotope Labeling - methods
Magnetic Resonance Spectroscopy - instrumentation
Magnetic Resonance Spectroscopy - methods
Nitrogen Isotopes
Oriented samples
Peptides - analysis
PISEMO
Proteins - analysis
Solid-state NMR
Spin Labels
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Description
Summary:By incorporating homonuclear decoupling on both the 1H and 13C channels it is feasible to obtain high-resolution two-dimensional separated local field spectra of peptides and proteins that are 100% labeled with 13C. Dual-PISEMO (Polarization Inversion Spin Exchange Modulated Observation) can be performed as a conventional two-dimensional experiment, or with windowed detection as a one-dimensional experiment that offers flexibility as a building block for shiftless and other multidimensional triple-resonance experiments with the inclusion of 15N irradiation. The triple-resonance MAGC probe used to perform these experiments at 500 MHz is described.
ISSN:1090-7807
1096-0856
DOI:10.1016/j.jmr.2010.06.011