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NMR processing:
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NMR assignment:
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Side-chains:
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NOEs:
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UNIO Candid
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
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Fragment-based:
BMRB CS-Rosetta
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Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
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MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
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Protein geomtery:
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What-If
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PSVS
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SAVES2 or SAVES4
Vadar
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MetaMQAPII
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Verify_3D
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NMR spectrum prediction:
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V-NMR
Flexibility from structure:
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Methyl S2
B-factor
Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
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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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Default Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.

Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.

Related Articles Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.

Angew Chem Int Ed Engl. 2012 Dec 21;51(52):13140-3

Authors: Madine J, Pandya MJ, Hicks MR, Rodger A, Yates EA, Radford SE, Middleton DA

Abstract
At the surface of A?(1-40) amyloid fibrils that have a threefold molecular symmetry (green in the left picture) a site of interaction of the glycosaminoglycan analogue heparin (blue) was identified. The binding site consists of residues at the N terminus and the turn regions defining the apices of the triangular geometry. Heparin has a lower affinity for A?(1-40) fibrils having twofold molecular symmetry, thus revealing a remarkable morphological selectivity.


PMID: 23161730 [PubMed - indexed for MEDLINE]



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