Related ArticlesCorrection to: The NMR contribution to protein-protein networking in Fe-S protein maturation.
J Biol Inorg Chem. 2018 May 31;:
Authors: Banci L, Camponeschi F, Ciofi-Baffoni S, Piccioli M
Abstract
The article "The NMR contribution to protein-protein networking in Fe-S protein maturation", written by Lucia Banci, Francesca Camponeschi, Simone Ciofi-Baffoni, Mario Piccioli was originally published electronically on the publisher's internet portal (currently SpringerLink) on 22 March, 2018 without open access.
PMID: 29855713 [PubMed - as supplied by publisher]
[NMR paper] The NMR contribution to protein-protein networking in Fe-S protein maturation.
The NMR contribution to protein-protein networking in Fe-S protein maturation.
The NMR contribution to protein-protein networking in Fe-S protein maturation.
J Biol Inorg Chem. 2018 Mar 22;:
Authors: Banci L, Camponeschi F, Ciofi-Baffoni S, Piccioli M
Abstract
Iron-sulfur proteins were among the first class of metalloproteins that were actively studied using NMR spectroscopy tailored to paramagnetic systems. The hyperfine shifts, their temperature dependencies and the relaxation rates of nuclei of cluster-bound residues are an...
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[NMR paper] Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
PLoS One. 2017;12(9):e0184487
Authors: Delius J, Frank O, Hofmann T
Abstract
Nuclear magnetic resonance (NMR) spectroscopy is well-established in assessing the binding affinity between...
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09-09-2017 06:59 PM
[NMR paper] Contribution of protein phosphorylation to binding-induced folding of the SLBP-histone mRNA complex probed by phosphorus-31 NMR.
Contribution of protein phosphorylation to binding-induced folding of the SLBP-histone mRNA complex probed by phosphorus-31 NMR.
Contribution of protein phosphorylation to binding-induced folding of the SLBP-histone mRNA complex probed by phosphorus-31 NMR.
FEBS Open Bio. 2014;4:853-7
Authors: Thapar R
Abstract
Phosphorus-31 ((31)P) NMR can be used to characterize the structure and dynamics of phosphorylated proteins. Here, I use (31)P NMR to report on the chemical nature of a phosphothreonine that lies in the RNA binding domain...
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Contribution of protein phosphorylation to binding-induced folding of the SLBP–histone mRNA complex probed by phosphorus-31 NMR
Contribution of protein phosphorylation to binding-induced folding of the SLBP–histone mRNA complex probed by phosphorus-31 NMR
Publication date: Available online 16 October 2014
Source:FEBS Open Bio</br>
Author(s): Roopa Thapar</br>
Phosphorus-31 (31P) NMR can be used to characterize the structure and dynamics of phosphorylated proteins. Here, I use 31P NMR to report on the chemical nature of a phosphothreonine that lies in the RNA binding domain of SLBP (stem-loop binding protein). SLBP is an intrinsically disordered protein and phosphorylation at this threonine...
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10-16-2014 01:09 PM
[NMR paper] Correction of erroneously packed protein's side chains in the NMR structure based on ab initio chemical shift calculations.
Correction of erroneously packed protein's side chains in the NMR structure based on ab initio chemical shift calculations.
Correction of erroneously packed protein's side chains in the NMR structure based on ab initio chemical shift calculations.
Phys Chem Chem Phys. 2014 Jul 23;
Authors: Zhu T, Zhang JZ, He X
Abstract
In this work, protein side chain (1)H chemical shifts are used as probes to detect and correct side-chain packing errors in protein's NMR structures through structural refinement. By applying the automated...
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07-24-2014 11:56 AM
[NMR paper] Atomic-resolution monitoring of protein maturation in live human cells by NMR.
Atomic-resolution monitoring of protein maturation in live human cells by NMR.
Atomic-resolution monitoring of protein maturation in live human cells by NMR.
Nat Chem Biol. 2013 Mar 3;
Authors: Banci L, Barbieri L, Bertini I, Luchinat E, Secci E, Zhao Y, Aricescu AR
Abstract
We use NMR directly in live human cells to describe the complete post-translational maturation process of human superoxide dismutase 1 (SOD1). We follow, at atomic resolution, zinc binding, homodimer formation and copper uptake, and discover that copper chaperone for...
[NMR paper] Membrane protein structure: the contribution and potential of novel solid state NMR a
Membrane protein structure: the contribution and potential of novel solid state NMR approaches.
Related Articles Membrane protein structure: the contribution and potential of novel solid state NMR approaches.
Mol Membr Biol. 1995 Jul-Sep;12(3):233-46
Authors: Watts A, Ulrich AS, Middleton DA
Alternative methods for describing molecular detail for large integral membrane proteins are required in the absence of routine crystallographic approaches. Novel solid state NMR methods, devised for the study of large molecular assemblies, are now finding...
Correction to: The NMR contribution to protein-protein networking in Fe-S protein maturation.
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