Biomedical Engineering Reference
In-Depth Information
CHAPTER 1
Isotope-Labelling of Methyl
Groups for NMR Studies of
Large Proteins
MICHAEL J. PLEVIN AND J ´ R ˆ ME BOISBOUVIER
CEA, Institut de Biologie Structurale, CNRS, Institut de Biologie Structurale
Jean-Pierre and Universit´ Joseph Fourier, Institut de Biologie Structurale
Jean-Pierre Ebel, Grenoble, France
E-mail: michael.plevin@ibs.fr or jerome.boisbouvier@ibs.fr
1.1
Introduction—Large Proteins and Solution NMR
Spectroscopy
1.1.1 Isotope-Labelling and Protein NMR Spectroscopy
Solution NMR spectroscopy is a well-established technique for characterising
the structure, function and dynamics of proteins at atomic resolution. Proteins
are predominantly composed of carbon, nitrogen, oxygen and hydrogen. Of
these four, only hydrogen has a naturally abundant, NMR-visible spin-K
nucleus and, for this reason, the proton was the major focus of early protein
NMR studies. One of the major drawbacks of proton NMR spectroscopy is
the inherent low dispersion of
1 H chemical shifts. The narrow range of
1 H
1 H
resonance frequencies means that the ability to differentiate individual
signals
becomes
increasingly
problematic
as
the
size
of
the
protein
and
therefore the number of potential signals increases.
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