NMR paper Using NMR spectroscopy to investigate the role played by copper in prion diseases.

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[NMR paper] Using NMR spectroscopy to investigate the role played by copper in prion diseases.

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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

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RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

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NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

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SAVES2 or SAVES4

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FANDAS

MestReS

V-NMR

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Backbone S2

Methyl S2

B-factor

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Camshift

CH3shift- Methyl

ArShift- Aromatic

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Proshift

PPM

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Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

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04-25-2020, 12:56 PM

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Using NMR spectroscopy to investigate the role played by copper in prion diseases.

Using NMR spectroscopy to investigate the role played by copper in prion diseases.

Related Articles Using NMR spectroscopy to investigate the role played by copper in prion diseases.

Neurol Sci. 2020 Apr 24;:

Authors: Alsiary RA, Alghrably M, Saoudi A, Al-Ghamdi S, Jaremko L, Jaremko M, Emwas AH

Abstract
Prion diseases are a group of rare neurodegenerative disorders that develop as a result of the conformational conversion of normal prion protein (PrPC) to the disease-associated isoform (PrPSc). The mechanism that actually causes disease remains unclear. However, the mechanism underlying the conformational transformation of prion protein is partially understood-in particular, there is strong evidence that copper ions play a significant functional role in prion proteins and in their conformational conversion. Various models of the interaction of copper ions with prion proteins have been proposed for the Cu (II)-binding, cell-surface glycoprotein known as prion protein (PrP). Changes in the concentration of copper ions in the brain have been associated with prion diseases and there is strong evidence that copper plays a significant functional role in the conformational conversion of PrP. Nevertheless, because copper ions have been shown to have both a positive and negative effect on prion disease onset, the role played by Cu (II) ions in these diseases remains a topic of debate. Because of the unique properties of paramagnetic Cu (II) ions in the magnetic field, their interactions with PrP can be tracked even at single atom resolution using nuclear magnetic resonance (NMR) spectroscopy. Various NMR approaches have been utilized to study the kinetic, thermodynamic, and structural properties of Cu (II)-PrP interactions. Here, we highlight the different models of copper interactions with PrP with particular focus on studies that use NMR spectroscopy to investigate the role played by copper ions in prion diseases.

PMID: 32328835 [PubMed - as supplied by publisher]

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