Biomolecular NMR using a microcoil NMR probe–new technique for the chemical shift assignment of aromatic side chains in proteins. Peti, W., Norcross, J., Eldridge, G., & O'Neil-Johnson, M. Journal of the American Chemical Society, 126(18):5873–5878, May, 2004. ![Biomolecular NMR using a microcoil NMR probe–new technique for the chemical shift assignment of aromatic side chains in proteins. [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex A specially designed microcoil probe for use in biomolecular NMR spectroscopy is presented. The microcoil probe shows a mass-based sensitivity increase of a minimal factor of 7.5, allowing for the first time routine biomolecular NMR spectroscopy with microgram amounts of proteins. In addition, the exceptional radio frequency capabilities of this probe allowed us to record an aliphatic-aromatic HCCH-TOCSY spectrum for the first time. Using this spectrum, the side chains of aliphatic and aromatic amino acids can be completely assigned using only a single experiment. Using the conserved hypothetical protein TM0979 from Thermotoga maritima, we demonstrate the capabilities of this microcoil NMR probe to completely pursue the sequence specific backbone assignment with less than 500 microg of (13)C,(15)N labeled protein.
@article{Peti2004,
title = {Biomolecular {NMR} using a microcoil {NMR} probe--new technique for the chemical shift assignment of aromatic side chains in proteins.},
volume = {126},
issn = {0002-7863},
url = {http://www.ncbi.nlm.nih.gov/pubmed/15125680},
doi = {10.1021/ja039779d},
abstract = {A specially designed microcoil probe for use in biomolecular NMR spectroscopy is presented. The microcoil probe shows a mass-based sensitivity increase of a minimal factor of 7.5, allowing for the first time routine biomolecular NMR spectroscopy with microgram amounts of proteins. In addition, the exceptional radio frequency capabilities of this probe allowed us to record an aliphatic-aromatic HCCH-TOCSY spectrum for the first time. Using this spectrum, the side chains of aliphatic and aromatic amino acids can be completely assigned using only a single experiment. Using the conserved hypothetical protein TM0979 from Thermotoga maritima, we demonstrate the capabilities of this microcoil NMR probe to completely pursue the sequence specific backbone assignment with less than 500 microg of (13)C,(15)N labeled protein.},
number = {18},
journal = {Journal of the American Chemical Society},
author = {Peti, Wolfgang and Norcross, James and Eldridge, Gary and O'Neil-Johnson, Mark},
month = may,
year = {2004},
pmid = {15125680},
keywords = {Bacterial Proteins, Bacterial Proteins: chemistry, Biomolecular, Biomolecular: instrume, Biomolecular: methods, Nuclear Magnetic Resonance, Thermotoga maritima, Thermotoga maritima: chemistry},
pages = {5873--5878},
}
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