NMR paper NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into diff

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[NMR paper] NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into diff

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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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08-22-2010, 03:31 PM

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NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into diff

NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into different sites of the maltose-binding protein.

Related Articles NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into different sites of the maltose-binding protein.

J Biol Chem. 1997 Jan 3;272(1):362-8

Authors: Lecroisey A, Martineau P, Hofnung M, Delepierre M

A set of permissive positions that tolerate insertions/deletions without major deleterious consequences for the binding activity of the protein was previously identified in the maltose-binding protein. The C3 epitope from poliovirus VP1 protein (93DNPASTTNKDK103) was inserted into eight of these positions and two nonpermissive control sites. NMR studies were performed on the MalE protein, the insertion/deletion mutants, and the C3MalE hybrids to selectively determine the flexible regions in these proteins. Comparison of the C3 epitope mobility in the different hybrid proteins indicates that, whatever its insertion site and independently from the specific sequences of its linkers, the epitope is mostly flexible. The vector protein was shown to unfold partially only in the two C3MalE hybrids that correspond to nonpermissive positions. For one of them (insertion at site 339), both sides of the insert are flexible, and at most one side for all the other hybrids. This result correlates with the antigenicity data on the inserted epitope (Martineau, P., Leclerc, C., and Hofnung, M. (1997) Mol. Immunol, in press.

PMID: 8995270 [PubMed - indexed for MEDLINE]

Source: PubMed

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