Wang, Sinan, David E. Korenchan, Paola M. Perez, Céline Taglang, Thomas R. Hayes, Renuka Sriram, Robert Bok, et al. “Amino Acid-Derived Sensors for Specific Zn2+ Detection Using Hyperpolarized 13C Magnetic Resonance Spectroscopy.” Chemistry – A European Journal 25, no. 51 (September 12, 2019): 11842–46.
Alterations in Zn2+ homeostasis have been targeted for diagnosis and treatment of human diseases including cancer, diabetes, and neurodegenerative illness. Herein, enriched [113C]cysteine and [1-13C2]iminodiacetic acid were developed as Zn2+specific imaging probes using hyperpolarized 13C magnetic resonance spectroscopy. [1-13C]cysteine was used to accurately quantify Zn2+ in complex biological mixtures. These sensors can be employed to detect Zn2+ via imaging mechanisms including changes in 13C chemical shift, resonance linewidth, or T1.
Hyperpolarized Multi-Metal 13C-Sensors for Magnetic Resonance Imaging
From The DNP-NMR Blog:
Hyperpolarized Multi-Metal 13C-Sensors for Magnetic Resonance Imaging
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Mishra, A., et al., Hyperpolarized Multi-Metal 13C-Sensors for Magnetic Resonance Imaging. Anal Chem, 2016. 88(22): p. 10790-10794.
https://www.ncbi.nlm.nih.gov/pubmed/27766840
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Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA)
Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA)
Abstract
The use of paramagnetic constraints in protein NMR is an active area of research because of the benefits of long-range distance measurements (>10Â*Ã?). One of the main issues in successful execution is the incorporation of a paramagnetic metal ion into diamagnetic proteins. The most common metal ion tags are relatively long aliphatic chains attached to the side chain of a...
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11-28-2014 11:37 AM
Hyperpolarized Xenon-Based Molecular Sensors for Label-Free Detection of analytes
From The DNP-NMR Blog:
Hyperpolarized Xenon-Based Molecular Sensors for Label-Free Detection of analytes
Garimella, P.D., et al., Hyperpolarized Xenon-Based Molecular Sensors for Label-Free Detection of analytes. J. Am. Chem. Soc., 2013. 136(1): p. 164-168.
http://pubs.acs.org/doi/abs/10.1021/ja406760r
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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
Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Magn Reson Chem. 2011 Feb;49(2):65-9
Authors: Middleton DA
Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the...
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01-22-2011 01:52 PM
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Magn Reson Chem. 2011 Jan 3;
Authors: Middleton DA
Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the secondary...
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01-05-2011 09:51 PM
[NMR paper] Amino acid-specific isotopic labeling and active site NMR studies of iron(II)- and ir
Amino acid-specific isotopic labeling and active site NMR studies of iron(II)- and iron(III)-superoxide dismutase from Escherichia coli.
Related Articles Amino acid-specific isotopic labeling and active site NMR studies of iron(II)- and iron(III)-superoxide dismutase from Escherichia coli.
J Biomol NMR. 2000 Aug;17(4):311-22
Authors: Sorkin DL, Miller AF
We have developed and employed multiple amino acid-specific isotopic labeling schemes to obtain definitive assignments for active site 1H NMR resonances of iron(II)- and iron(III)-superoxide...
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11-19-2010 08:29 PM
[NMR paper] Application of amino acid type-specific 1H- and 14N-labeling in a 2H-, 15N-labeled ba
Application of amino acid type-specific 1H- and 14N-labeling in a 2H-, 15N-labeled background to a 47 kDa homodimer: potential for NMR structure determination of large proteins.
Related Articles Application of amino acid type-specific 1H- and 14N-labeling in a 2H-, 15N-labeled background to a 47 kDa homodimer: potential for NMR structure determination of large proteins.
J Biomol NMR. 1999 May;14(1):79-83
Authors: Kelly MJ, Krieger C, Ball LJ, Yu Y, Richter G, Schmieder P, Bacher A, Oschkinat H
NMR investigations of larger macromolecules (> 20...
Amino Acid-Derived Sensors for Specific Zn2+ Detection Using Hyperpolarized 13C Magnetic Resonance Spectroscopy #DNPNMR
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