Homonuclear dipolar recoupling techniques for structure determination in uniformly 13C-labeled proteins.

Homonuclear dipolar recoupling techniques for structure determination in uniformly 13C-labeled proteins. Ladizhansky, V. Solid state nuclear magnetic resonance, 36(3):119–128, November, 2009. ISBN: 09262040

Paper doi abstract bibtex

In solid-state NMR magic angle spinning is often used to remove line broadening associated with anisotropic interactions, such as chemical shift anisotropy and dipolar couplings. Dipolar recoupling refers to sequences of pulses designed to reintroduce dipolar interactions that are otherwise averaged by magic angle spinning. One of the key applications of homonuclear (and heteronuclear) dipolar recoupling is for the purpose of protein structure determination. Recoupling experiments, originally designed for applications in spin-pair labeled samples, have been revised in recent years for applications in samples with extensive or uniform incorporation of isotopic labels. In these samples multiple internuclear distances can in principle be probed simultaneously, but the dipolar truncation effects (i.e. attenuation of the effects of weak couplings by strong ones) circumvent such measurements. In this article we review some of the recent developments in homonuclear recoupling methods that allow overcoming this problem.

@article{Ladizhansky2009,
	title = {Homonuclear dipolar recoupling techniques for structure determination in uniformly {13C}-labeled proteins.},
	volume = {36},
	issn = {1527-3326},
	url = {http://www.ncbi.nlm.nih.gov/pubmed/19729285},
	doi = {10.1016/j.ssnmr.2009.07.003},
	abstract = {In solid-state NMR magic angle spinning is often used to remove line broadening associated with anisotropic interactions, such as chemical shift anisotropy and dipolar couplings. Dipolar recoupling refers to sequences of pulses designed to reintroduce dipolar interactions that are otherwise averaged by magic angle spinning. One of the key applications of homonuclear (and heteronuclear) dipolar recoupling is for the purpose of protein structure determination. Recoupling experiments, originally designed for applications in spin-pair labeled samples, have been revised in recent years for applications in samples with extensive or uniform incorporation of isotopic labels. In these samples multiple internuclear distances can in principle be probed simultaneously, but the dipolar truncation effects (i.e. attenuation of the effects of weak couplings by strong ones) circumvent such measurements. In this article we review some of the recent developments in homonuclear recoupling methods that allow overcoming this problem.},
	number = {3},
	journal = {Solid state nuclear magnetic resonance},
	author = {Ladizhansky, Vladimir},
	month = nov,
	year = {2009},
	pmid = {19729285},
	note = {ISBN: 09262040},
	keywords = {Anisotropy, Biomolecular, Biomolecular: methods, Carbon Isotopes, Nuclear Magnetic Resonance, Proteins, Proteins: chemistry, Protons, Rotation},
	pages = {119--128},
}

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