NMR paper Chemical Synthesis of the Highly Hydrophobic Antiviral Membrane Associated Protein IFITM3 and Modified Variants

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[NMR paper] Chemical Synthesis of the Highly Hydrophobic Antiviral Membrane Associated Protein IFITM3 and Modified Variants

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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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08-21-2017, 02:23 PM

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Chemical Synthesis of the Highly Hydrophobic Antiviral Membrane Associated Protein IFITM3 and Modified Variants

Chemical Synthesis of the Highly Hydrophobic Antiviral Membrane Associated Protein IFITM3 and Modified Variants

Interferon-induced transmembrane protein 3 (IFITM3) is an antiviral transmembrane protein thought to serve as the primary factor for inhibiting replication of a large number of viruses, including the West Nile virus, the Dengue virus, the Ebola virus, and the Zika virus. Production of this 14.5 kDa, 133-residue, transmembrane protein, especially with essential posttranslational modifications by recombinant expression is challenging. In this report, we document the chemical synthesis of IFTIM3 in multimilligram quantities (>15 mg) and the preparation of phosphorylated and fluorescent variants. The synthesis was accomplished by KAHA ligations, which operate under acidic aqueous/organic mixtures that excel at solubilizing even the exceptionally hydrophobic C-terminal region of IFITM3. The synthetic material readily incorporates in model vesicles and forms the basis for using synthetic, homogenous IFITM3 and its derivatives for further studying its structure and biological mode of action.

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