Laser-assisted NMR in the Presence of a Cryogenic Probe Enables Multidimensional Data Collection on Amino Acids and Proteins at Unprecedented Sensitivity
Laser-assisted NMR in the Presence of a Cryogenic Probe Enables Multidimensional Data Collection on Amino Acids and Proteins at Unprecedented Sensitivity
[NMR paper] Facilitating unambiguous NMR assignments and enabling higher probe density through selective labeling of all methyl containing amino acids.
Facilitating unambiguous NMR assignments and enabling higher probe density through selective labeling of all methyl containing amino acids.
Related Articles Facilitating unambiguous NMR assignments and enabling higher probe density through selective labeling of all methyl containing amino acids.
J Biomol NMR. 2016 Apr 29;
Authors: Proudfoot A, Frank AO, Ruggiu F, Mamo M, Lingel A
Abstract
The deuteration of proteins and selective labeling of side chain methyl groups has greatly enhanced the molecular weight range of proteins...
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05-01-2016 10:32 PM
Facilitating unambiguous NMR assignments and enabling higher probe density through selective labeling of all methyl containing amino acids
Facilitating unambiguous NMR assignments and enabling higher probe density through selective labeling of all methyl containing amino acids
Abstract
The deuteration of proteins and selective labeling of side chain methyl groups has greatly enhanced the molecular weight range of proteins and protein complexes which can be studied using solution NMR spectroscopy. Protocols for the selective labeling of all six methyl group containing amino acids individually are available, however to date, only a maximum of five amino acids have been labeled...
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04-30-2016 09:26 AM
[NMR paper] Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets.
Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets.
Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets.
J Biomol NMR. 2013 Aug 14;
Authors: Bellstedt P, Seiboth T, Häfner S, Kutscha H, Ramachandran R, Görlach M
Abstract
NMR-based structure determination of a protein requires the assignment of resonances as indispensable first step. Even though...
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08-15-2013 07:45 PM
[NMR paper] Photo-CIDNP NMR Spectroscopy of Amino Acids and Proteins.
Photo-CIDNP NMR Spectroscopy of Amino Acids and Proteins.
Related Articles Photo-CIDNP NMR Spectroscopy of Amino Acids and Proteins.
Top Curr Chem. 2013 May 14;
Authors: Kuhn LT
Abstract
Photo-chemically induced dynamic nuclear polarization (CIDNP) is a nuclear magnetic resonance (NMR) phenomenon which, among other things, is exploited to extract information on biomolecular structure via probing solvent-accessibilities of tryptophan (Trp), tyrosine (Tyr), and histidine (His) amino acid side chains both in polypeptides and proteins in...
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05-15-2013 03:12 PM
Site-specific labeling of proteins with NMR-active unnatural amino acids
Site-specific labeling of proteins with NMR-active unnatural amino acids
Abstract A large number of amino acids other than the canonical amino acids can now be easily incorporated in vivo into proteins at genetically encoded positions. The technology requires an orthogonal tRNA/aminoacyl-tRNA synthetase pair specific for the unnatural amino acid that is added to the media while a TAG amber or frame shift codon specifies the incorporation site in the protein to be studied. These unnatural amino acids can be isotopically labeled and provide unique opportunities for site-specific labeling...
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01-09-2011 12:46 PM
[NMR paper] High-resolution iterative frequency identification for NMR as a general strategy for multidimensional data collection.
High-resolution iterative frequency identification for NMR as a general strategy for multidimensional data collection.
Related Articles High-resolution iterative frequency identification for NMR as a general strategy for multidimensional data collection.
J Am Chem Soc. 2005 Sep 14;127(36):12528-36
Authors: Eghbalnia HR, Bahrami A, Tonelli M, Hallenga K, Markley JL
We describe a novel approach to the rapid collection and processing of multidimensional NMR data: "high-resolution iterative frequency identification for NMR" (HIFI-NMR). As with...
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12-01-2010 06:56 PM
[NMR paper] Assigning the NMR spectra of aromatic amino acids in proteins: analysis of two Ets po
Assigning the NMR spectra of aromatic amino acids in proteins: analysis of two Ets pointed domains.
Related Articles Assigning the NMR spectra of aromatic amino acids in proteins: analysis of two Ets pointed domains.
Biochem Cell Biol. 1998;76(2-3):379-90
Authors: Slupsky CM, Gentile LN, McIntosh LP
The measurement of interproton nuclear Overhauser enhancements (NOEs) and dihedral angle restraints of aromatic amino acids is a critical step towards determining the structure of a protein. The complete assignment of the resonances from aromatic...
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11-17-2010 11:06 PM
[NMR paper] Determination of de novo synthesized amino acids in cellular proteins revisited by 13
Determination of de novo synthesized amino acids in cellular proteins revisited by 13C NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Determination of de novo synthesized amino acids in cellular proteins revisited by 13C NMR spectroscopy.
NMR Biomed. 1997 Apr;10(2):50-8
Authors: Flögel U, Willker W, Leibfritz D
13C nuclear magnetic resonance spectroscopy was used to determine the absolute amounts to de novo...
Laser-assisted NMR in the Presence of a Cryogenic Probe Enables Multidimensional Data Collection on Amino Acids and Proteins at Unprecedented Sensitivity
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