NMR paper NMR probing of protein-protein interactions using reporter ligands and affinity tags.

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[NMR paper] NMR probing of protein-protein interactions using reporter ligands and affinity tags.

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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, 09:25 PM

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NMR probing of protein-protein interactions using reporter ligands and affinity tags.

NMR probing of protein-protein interactions using reporter ligands and affinity tags.

Related Articles NMR probing of protein-protein interactions using reporter ligands and affinity tags.

J Am Chem Soc. 2004 Feb 18;126(6):1636-7

Authors: Ludwiczek ML, Baminger B, Konrat R

A novel method is proposed for the detection and quantification of protein-protein interactions in solution. In this approach, one protein binding partner is tagged with a ligand binding domain, and protein-protein interaction is monitored via changes in the NMR relaxation of a reporter ligand which reversibly binds to the ligand binding domain. The particular benefit of the method is that only minute amounts of protein material and no isotope labeling are required. Its ease of implementation and the high-throughput capabilities make the method an attractive complement to existing proteomic methodology.

PMID: 14871086 [PubMed - indexed for MEDLINE]

Source: PubMed

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