Translocator protein (TSPO, 18 kDa), previously known as peripheral-type benzodiazepine receptor, is an evolutionarily conserved membrane protein involved in various physiological processes and patho-physiological conditions. The endogeneous TSPO ligand is a polypeptide of 9 kDa, but dipeptides with biological activity have been previously synthesized and characterized. Herein, we synthesized a phenyl alanine derived ligand with a ^(19)F labelling which opens prospective for ^(19)F-MRI and...
[NMR paper] Solid-state NMR study of structural heterogeneity of the apo WT mouse TSPO reconstituted in liposomes
Solid-state NMR study of structural heterogeneity of the apo WT mouse TSPO reconstituted in liposomes
In the last decades, ligand binding to human TSPO has been largely used in clinical neuroimaging, but little is known about the interaction mechanism. Protein conformational mobility plays a key role in the ligand recognition and both, ligand-free and ligand-bound structures, are mandatory for characterizing the molecular binding mechanism. In the absence of crystals for mammalian TSPO, we have exploited solid-state nuclear magnetic resonance (ssNMR) spectroscopy under magic-angle spinning...
Amino Acid-Derived Sensors for Specific Zn2+ Detection Using Hyperpolarized 13C Magnetic Resonance Spectroscopy #DNPNMR
From The DNP-NMR Blog:
Amino Acid-Derived Sensors for Specific Zn2+ Detection Using Hyperpolarized 13C Magnetic Resonance Spectroscopy #DNPNMR
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.
https://doi.org/10.1002/chem.201902771.
[NMR paper] Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study.
Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study.
Related Articles Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study.
Sci Rep. 2017 Sep 04;7(1):10339
Authors: Mukherjee S, Pondaven SP, Hand K, Madine J, Jaroniec CP
Abstract
The conformational dynamics of a pathogenic ?4 human immunoglobulin light-chain variable domain, SMA, associated with AL...
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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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[NMR paper] The Involvement of Amino Acid Side Chains in Shielding the Nickel Coordination Site: An NMR Study.
The Involvement of Amino Acid Side Chains in Shielding the Nickel Coordination Site: An NMR Study.
The Involvement of Amino Acid Side Chains in Shielding the Nickel Coordination Site: An NMR Study.
Molecules. 2013;18(10):12396-12414
Authors: Medici S, Peana M, Nurchi VM, Zoroddu MA
Abstract
Coordination of proteins and peptides to metal ions is known to affect their properties, often by a change in their structural organization. Side chains of the residues directly involved in metal binding or very close to the coordination centre...
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[NMR paper] Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
Related Articles Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
J Biol Chem. 2013 Jan 22;
Authors: De Sa Peixoto P, Laurent G, Azais T, Mosser G
Abstract
In vivo, collagen I, the major structural protein in human body, is found assembled into fibrils. In the present work, we study a high concentrated collagen sample in its soluble, fibrillar and denatured states...
Fluor NMR study of amino acid derived ligand to study TSPO
Linear Mode
