NMR paper G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment

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[NMR paper] G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment

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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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11-24-2010, 09:51 PM

nmrlearner

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G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment

G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment.

Related Articles G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment.

Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9642-7

Authors: Atreya HS, Szyperski T

A G-matrix Fourier transform (GFT) NMR spectroscopy-based strategy for resonance assignment of proteins is described. Each of the GFT NMR experiments presented here rapidly affords four-, five-, or six-dimensional spectral information in combination with precise measurements of chemical shifts. The resulting high information content enables one to obtain nearly complete assignments by using only four NMR experiments. For the backbone amide proton detected "out-and-back" experiments, data collection was further accelerated up to approximately 2.5-fold by use of longitudinal (1)H relaxation optimization. The GFT NMR experiments were acquired for three proteins with molecular masses ranging from 8.6 to 17 kDa, demonstrating that the proposed strategy is of key interest for automated resonance assignment in structural genomics.

PMID: 15210958 [PubMed - indexed for MEDLINE]

Source: PubMed

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