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 efficient fingerprint of the nature and the oxidation state of the Fe-S cluster. NMR significantly contributed to the analysis of the magnetic coupling patterns and to the understanding of the electronic structure occurring in [2Fe-2S], [3Fe-4S] and [4Fe-4S] clusters bound to proteins. After the first NMR structure of a paramagnetic protein was obtained for the reduced E. halophila HiPIP I, many NMR structures were determined for several Fe-S proteins in different oxidation states. It was found that differences in chemical shifts, in patterns of unobserved residues, in internal mobility and in thermodynamic stability are suitable data to map subtle changes between the two different oxidation states of the protein. Recently, the interaction networks responsible for maturing human mitochondrial and cytosolic Fe-S proteins have been largely characterized by combining solution NMR standard experiments with those tailored to paramagnetic systems. We show here the contribution of solution NMR in providing a detailed molecular view of "Fe-S interactomics". This contribution was particularly effective when protein-protein interactions are weak and transient, and thus difficult to be characterized at high resolution with other methodologies.
PMID: 29569085 [PubMed - as supplied by publisher]
[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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[NMR paper] Structural and Biochemical Analysis of Protein–Protein Interactions Between the Acyl-Carrier Protein and Product Template Domain
Structural and Biochemical Analysis of Protein–Protein Interactions Between the Acyl-Carrier Protein and Product Template Domain
In fungal non-reducing polyketide synthases (NR-PKS) the acyl-carrier protein (ACP) carries the growing polyketide intermediate through iterative rounds of elongation, cyclization and product release. This process occurs through a controlled, yet enigmatic coordination of the ACP with its partner enzymes. The transient nature of ACP interactions with these catalytic domains imposes a major obstacle for investigation of the influence of protein–protein...
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09-22-2016 10:41 PM
Postdoc in protein biophysics / NMR to study protein-protein, protein-lipid ... - Scientific American
Postdoc in protein biophysics / NMR to study protein-protein, protein-lipid ... - Scientific American
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Postdoc in protein biophysics / NMR to study protein-protein, protein-lipid ...
Scientific American
How are signaling events transmitted from one protein to another and especially through the lipid bilayer? To answer these questions we are looking to add a postdoctoral co-worker to our interdisciplinary team. Our interest is to understand protein ...
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11-23-2014 03:59 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] 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...
The NMR contribution to protein-protein networking in Fe-S protein maturation.
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