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NMR processing:
MDD
NMR assignment:
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MARS
UNIO Match
PINE
Side-chains:
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NOEs:
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UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
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Chemical shifts:
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RDCs:
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Pseudocontact shifts:
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Protein geomtery:
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What-If
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PSVS
MolProbity
SAVES2 or SAVES4
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Verify_3D
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NMR spectrum prediction:
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V-NMR
Flexibility from structure:
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Methyl S2
B-factor
Molecular dynamics:
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Antechamber
Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
Shifty
Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
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Old 02-13-2013, 12:47 PM
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Default Site-specific interaction between ?-synuclein and membranes probed by NMR-observed methionine oxidation rates.

Site-specific interaction between ?-synuclein and membranes probed by NMR-observed methionine oxidation rates.

Related Articles Site-specific interaction between ?-synuclein and membranes probed by NMR-observed methionine oxidation rates.

J Am Chem Soc. 2013 Feb 11;

Authors: Maltsev AS, Chen J, Levine RL, Bax A

Abstract
?-Synuclein (aS) is an intrinsically disordered protein that is water soluble but also can bind negatively charged lipid membranes while adopting an ?-helical conformation. Membrane affinity is increased by post-translational N-terminal acetylation, a common modification in all eukaroytic cells. In the presence of lipid vesicles containing a small fraction of peroxidized lipids, the N-terminal Met residues in aS (Met1 and Met5) rapidly oxidize while reducing the toxic lipid hydroperoxide to a non-reactive lipid hydroxide, whereas C-terminal Met residues remain unaffected. Met oxidation can be probed conveniently and quantitatively by NMR spectroscopy. Results show that oxidation of Met1 reduces the oxidation rate of Met5, and vice versa, caused by decreased membrane affinity of the partially oxidized protein. The effect of Met oxidation on aS-membrane affinity extends over large distances, with the oxidation rate of Met49 in the V49M mutant of aS being strongly impacted by oxidation states of Met1 and Met5, and inversely the oxidation state of Met49 affecting the oxidation rates of the N-terminal Met residues. When not bound to membrane, oxidized Met1 and Met5 of aS are excellent substrates for methionine sulfoxide reductase (Msr), thereby providing an efficient vehicle for water-soluble Msr enzymes to protect the membrane against oxidative damage.


PMID: 23398174 [PubMed - as supplied by publisher]



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