NMR paper 1H NMR study of the interaction of N,N',N"-triacetyl chitotriose with Ac-AMP2, a suga

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[NMR paper] 1H NMR study of the interaction of N,N',N"-triacetyl chitotriose with Ac-AMP2, a suga

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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, 03:50 AM

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1H NMR study of the interaction of N,N',N"-triacetyl chitotriose with Ac-AMP2, a suga

1H NMR study of the interaction of N,N',N"-triacetyl chitotriose with Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.

Related Articles 1H NMR study of the interaction of N,N',N"-triacetyl chitotriose with Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.

FEBS Lett. 1995 Aug 21;370(3):245-9

Authors: Verheyden P, Pletinckx J, Maes D, Pepermans HA, Wyns L, Willem R, Martins JC

The interaction between Ac-AMP2, a lectin-like small protein with antimicrobial and antifungal activity isolated from Amaranthus caudatus, and N,N',N"-triacetyl chitotriose was studied using 1H NMR spectroscopy. Changes in chemical shift and line width upon increasing concentration of N,N',N"-triacetyl chitotriose to Ac-AMP2 solutions at pH 6.9 and 2.4 were used to determine the interaction site and the association constant Ka. The most pronounced shifts occur mainly in the C-terminal half of the sequence. They involve the aromatic residues Phe18, Tyr20 and Tyr27 together with their surrounding residues, as well as the N-terminal Val-Gly-Glu segment. Several NOEs between Ac-AMP2 and the N,N',N"-triacetyl chitotriose resonances are reported.

PMID: 7656986 [PubMed - indexed for MEDLINE]

Source: PubMed

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