NMR paper Site-specific detection of arginine methylation in highly repetitive protein motifs of low sequence complexity by NMR.

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[NMR paper] Site-specific detection of arginine methylation in highly repetitive protein motifs of low sequence complexity by NMR.

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

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:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

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:

Isotope labeling:

Solid-state NMR:

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04-03-2020, 09:41 PM

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Site-specific detection of arginine methylation in highly repetitive protein motifs of low sequence complexity by NMR.

Related Articles Site-specific detection of arginine methylation in highly repetitive protein motifs of low sequence complexity by NMR.

J Am Chem Soc. 2020 Apr 01;:

Authors: Altincekic N, L?hr F, Meier-Credo J, Langer JD, Hengesbach M, Richter C, Schwalbe H

Abstract
Post-translational modifications of proteins are widespread in eukaryotes. To elucidate the functional role of these modifi-cations, detection methods need to be developed that provide information at atomic resolution. Here, we report on the de-velopment of a novel Arg-specific NMR-experiment that detects the methylation status and symmetry of each arginine side chain even in highly repetitive RGG amino acid sequence motifs found in numerous proteins within intrinsically disordered regions. The experiment relies on the excellent resolution of the backbone H,N correlation spectra even in these low com-plexity sequences. It requires 13C, 15N labeled samples.

PMID: 32233470 [PubMed - as supplied by publisher]

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