A new approach for rapid resonance assignments in proteins based on amino acid selective unlabeling can augment existing approaches and will be useful for identifying active-site residues involved in ligand binding, phosphorylation, or protein–protein interactions.
[NMR paper] Rapid NMR assignments of proteins using optimized combinatorial selective unlabeling.
Rapid NMR assignments of proteins using optimized combinatorial selective unlabeling.
Rapid NMR assignments of proteins using optimized combinatorial selective unlabeling.
Chembiochem. 2015 Dec 10;
Authors: Atreya HS, Dubey A, Jaipuria G, Kadumuri RV, Vadrevu R
Abstract
A new approach for rapid resonance assignments in proteins based on amino acid selective unlabeling is presented. The method involves choosing a set of multiple amino acid types for selective unlabeling and identifying specific tri-peptides surrounding the...
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12-15-2015 08:09 PM
[NMR paper] Amino Acid Selective Unlabeling in Protein NMR Spectroscopy.
Amino Acid Selective Unlabeling in Protein NMR Spectroscopy.
Related Articles Amino Acid Selective Unlabeling in Protein NMR Spectroscopy.
Methods Enzymol. 2015;565:167-189
Authors: Prasanna C, Dubey A, Atreya HS
Abstract
Three-dimensional structure determination of proteins by NMR requires the acquisition of multidimensional spectra followed by assignment of chemical shifts to the respective nuclei. In order to speed up this process, resonances corresponding to individual amino acid types are often selectively identified...
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11-19-2015 05:22 PM
Journal Highlight: Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy
Journal Highlight: Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy
http://www.spectroscopynow.com/common/images/thumbnails/14fff98e0e1.jpgRecent progress in the solid-state NMR spectroscopy of membrane proteins within a cellular membrane has been reviewed, along with requirements for sample preparation.
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09-28-2015 06:31 PM
Journal Highlight: Rapid assessment of the illegal presence of 1,3-dimethylamylamine (DMAA) in sports nutrition and dietary supplements using 1H NMR spectroscopy
Journal Highlight: Rapid assessment of the illegal presence of 1,3-dimethylamylamine (DMAA) in sports nutrition and dietary supplements using 1H NMR spectroscopy
http://www.spectroscopynow.com/common/images/thumbnails/14898526bb5.jpgA proton NMR method was developed and validated for measuring 1,3-dimethylamylamine in sports nutrition and dietary supplements and is recommended for routine use in food testing, customs or doping control laboratories.
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10-06-2014 12:37 PM
Journal Highlight: Assessment of higher order structure comparability in therapeutic proteins using nuclear magnetic resonance spectroscopy
Journal Highlight: Assessment of higher order structure comparability in therapeutic proteins using nuclear magnetic resonance spectroscopy
http://www.spectroscopynow.com/common/images/thumbnails/13ef9b3d882.jpgNMR spectroscopy using a fingerprinting approach has been used to rapidly assess higher order structure comparability in three nonglycosylated proteins spanning a molecular weight range of 6.5–67 kDa.
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06-03-2013 04:21 PM
Amino acid selective unlabeling for sequence specific resonance assignments in proteins
Amino acid selective unlabeling for sequence specific resonance assignments in proteins
Abstract Sequence specific resonance assignment constitutes an important step towards high-resolution structure determination of proteins by NMR and is aided by selective identification and assignment of amino acid types. The traditional approach to selective labeling yields only the chemical shifts of the particular amino acid being selected and does not help in establishing a link between adjacent residues along the polypeptide chain, which is important for sequential assignments. An alternative...
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03-20-2012 12:42 AM
[NMR paper] A combinatorial selective labeling method for the assignment of backbone amide NMR re
A combinatorial selective labeling method for the assignment of backbone amide NMR resonances.
Related Articles A combinatorial selective labeling method for the assignment of backbone amide NMR resonances.
J Am Chem Soc. 2004 Apr 28;126(16):5020-1
Authors: Parker MJ, Aulton-Jones M, Hounslow AM, Craven CJ
A combinatorial selective labeling (CSL) method is presented for the assignment of backbone amide NMR resonances, which has a particular application in the identification of protein-ligand interaction sites. The method builds on the dual...
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11-24-2010 09:51 PM
[NMR paper] Selective 'unlabeling' of amino acids in fractionally 13C labeled proteins: an approa
Selective 'unlabeling' of amino acids in fractionally 13C labeled proteins: an approach for stereospecific NMR assignments of CH3 groups in Val and Leu residues.
Related Articles Selective 'unlabeling' of amino acids in fractionally 13C labeled proteins: an approach for stereospecific NMR assignments of CH3 groups in Val and Leu residues.
J Biomol NMR. 2001 Mar;19(3):267-72
Authors: Atreya HS, Chary KV
A novel methodology for stereospecific NMR assignments of methyl (CH3) groups of Val and Leu residues in fractionally 13C-labeled proteins is...
Journal Highlight: Rapid NMR assignments of proteins by using optimized combinatorial selective unlabeling
A new approach for rapid resonance assignments in proteins based on amino acid selective unlabeling can augment existing approaches and will be useful for identifying active-site residues involved in ligand binding, phosphorylation, or protein–protein interactions.
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