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NMR processing:
MDD
NMR assignment:
Backbone:
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MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
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)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
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CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
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Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Default Insights on the Interaction between Transthyretin and A? in Solution. A Saturation Transfer Difference (STD) NMR Analysis of the Role of Iododiflunisal.

Insights on the Interaction between Transthyretin and A? in Solution. A Saturation Transfer Difference (STD) NMR Analysis of the Role of Iododiflunisal.

Related Articles Insights on the Interaction between Transthyretin and A? in Solution. A Saturation Transfer Difference (STD) NMR Analysis of the Role of Iododiflunisal.

J Med Chem. 2017 Jul 13;60(13):5749-5758

Authors: Gimeno A, Santos LM, Alemi M, Rivas J, Blasi D, Cotrina EY, Llop J, Valencia G, Cardoso I, Quintana J, Arsequell G, Jiménez-Barbero J

Abstract
Several strategies against Alzheimer disease (AD) are directed to target A?-peptides. The ability of transthyretin (TTR) to bind A?-peptides and the positive effect exerted by some TTR stabilizers for modulating the TTR-A? interaction have been previously studied. Herein, key structural features of the interaction between TTR and the A?(12-28) peptide (3), the essential recognition element of A?, have been unravelled by STD-NMR spectroscopy methods in solution. Molecular aspects related to the role of the TTR stabilizer iododiflunisal (IDIF, 5) on the TTR-A? complex have been also examined. The NMR results, assisted by molecular modeling protocols, have provided a structural model for the TTR-A? interaction, as well as for the ternary complex formed in the presence of IDIF. This basic structural information could be relevant for providing light on the mechanisms involved in the ameliorating effects of AD symptoms observed in AD/TTR(±) animal models after IDIF treatment and eventually for designing new molecules toward AD therapeutic drugs.


PMID: 28587455 [PubMed - indexed for MEDLINE]



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