[ASAP] Picometer Resolution Structure of the Coordination Sphere in the Metal-Binding Site in a Metalloprotein by NMR
Picometer Resolution Structure of the Coordination Sphere in the Metal-Binding Site in a Metalloprotein by NMR
Andrea Bertarello, Ladislav Benda, Kevin J. Sanders, Andrew J. Pell, Michael J. Knight, Vladimir Pelmenschikov, Leonardo Gonnelli, Isabella C. Felli, Martin Kaupp, Lyndon Emsley, Roberta Pierattelli, and Guido Pintacuda
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.0c07339/20200919/images/medium/ja0c07339_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.0c07339...
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[NMR paper] Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.
Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.
Eur Biophys J. 2017 Apr;46(3):293-300
Authors: Usachev KS, Kolosova OA, Klochkova EA, Yulmetov AR,...
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03-21-2017 11:26 PM
Transient iron coordination sites in proteins: exploiting the dual nature of paramagnetic NMR
Transient iron coordination sites in proteins: exploiting the dual nature of paramagnetic NMR
Publication date: Available online 22 May 2014
Source:Coordination Chemistry Reviews</br>
Author(s): Mario Piccioli , Paola Turano</br>
We provide here an historical perspective of NMR applied to iron-containing proteins. At first, the field developed using paramagnetic NMR: the 1H-NMR spectra of heme and FeS proteins were used as clear spectroscopic fingerprints of the electronic structure of the metal ion and its inner and outer coordination spheres. Starting 1994, NMR...
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05-22-2014 02:22 PM
Pb-207 NMR Spectroscopy Reveals that Pb(II) Coordinates with Glutathione (GSH) and Tris Cysteine Zinc Finger Proteins in a PbS(3) Coordination Environment.
Pb-207 NMR Spectroscopy Reveals that Pb(II) Coordinates with Glutathione (GSH) and Tris Cysteine Zinc Finger Proteins in a PbS(3) Coordination Environment.
Pb-207 NMR Spectroscopy Reveals that Pb(II) Coordinates with Glutathione (GSH) and Tris Cysteine Zinc Finger Proteins in a PbS(3) Coordination Environment.
J Inorg Biochem. 2011 Aug 1;105(8):1030-1034
Authors: Neupane KP, Pecoraro VL
(207)Pb NMR spectroscopy can be used to monitor the binding of Pb(II) to thiol rich biological small molecules such as glutathione and to zinc finger proteins. The...
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06-01-2011 02:30 PM
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Abstract Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties with achieving proper folding, membrane insertion, and native-like post-translational modifications frequently disqualify bacterial expression systems. On the other hand, eukaryotic cell cultures can be prohibitively expensive. One of the viable alternatives,...
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01-22-2011 03:46 AM
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
J Biomol NMR. 2011 Jan 19;
Authors: Fan Y, Shi L, Ladizhansky V, Brown LS
Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties...
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01-21-2011 01:22 AM
[NMR paper] An NMR view of the unfolding process of rusticyanin: Structural elements that maintain the architecture of a beta-barrel metalloprotein.
An NMR view of the unfolding process of rusticyanin: Structural elements that maintain the architecture of a beta-barrel metalloprotein.
Related Articles An NMR view of the unfolding process of rusticyanin: Structural elements that maintain the architecture of a beta-barrel metalloprotein.
Protein Sci. 2005 Jul;14(7):1710-22
Authors: Alcaraz LA, Jiménez B, Moratal JM, Donaire A
The unfolding process of the blue copper protein rusticyanin (Rc) as well as its dynamic and D(2)O/H(2)O exchange properties in an incipient unfolded state have been...
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[NMR paper] High-resolution polypeptide structure in a lamellar phase lipid environment from soli
High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints.
Related Articles High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints.
Structure. 1997 Dec 15;5(12):1655-69
Authors: Ketchem R, Roux B, Cross T
BACKGROUND: Solid-state nuclear magnetic resonance (NMR) spectroscopy provides novel structural constraints from uniformly aligned samples. These orientational constraints orient specific atomic...
A High-Resolution View of the Coordination Environment in a Paramagnetic Metalloprotein from its Magnetic Properties
Linear Mode
