NMR paper A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus.

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[NMR paper] A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus.

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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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11-11-2015, 02:40 PM

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A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus.

A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus.

Related Articles A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus.

Chem Commun (Camb). 2015 Nov 10;

Authors: Mallagaray A, Domínguez G, Peters T, Pérez-Castells J

Abstract
Attachment of human noroviruses to histo blood group antigens is thought to be essential for infection of host cells. Molecular details of the attachment process can be studied in vitro using a variety of NMR experiments. The use of protein NMR based experiments requires assignments of backbone NMR signals. Using uniformly (2)H,(15)N-labeled protruding domains (P-dimers) of a prevalent epidemic human norovirus strain (GII.4 Saga) we have studied the potential of ?-l-fucose covalently linked to a rigid lanthanide binding tag to aid backbone assignments using the paramagnetic properties of lanthanide ions. The synthesis of tagged ?-l-fucose is reported. Notably, the metal chelating unit connects to the carbohydrate via a triazole linker constructed using click chemistry.

PMID: 26553572 [PubMed - as supplied by publisher]

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