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

		BioNMR > Educational resources > Journal club
[NMR paper] Using NMR spectroscopy to investigate the role played by copper in prion diseases.

Webservers

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:

Thread Tools

Search this Thread

Rate Thread

Display Modes

04-25-2020, 12:56 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,777

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

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]

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Journal Highlight: Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases Journal Highlight: Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases http://www.spectroscopynow.com/common/images/thumbnails/13e5065f06a.jpgCurrent research on the role of copper in the conformational changes associated with prion diseases are reviewed with emphasis on the latest applications of NMR and EPR spectroscopy to probe the interactions of copper with prion proteins. Read the rest at Spectroscopynow.com	nmrlearner	General	0	04-29-2013 06:02 PM
[NMR paper] Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases. Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases. Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases. Magn Reson Chem. 2013 Feb 24; Authors: Emwas AH, Al-Talla ZA, Guo X, Al-Ghamdi S, Al-Masri HT Abstract Copper is an essential nutrient for the normal development of the brain and nervous system, although the hallmark of several neurological diseases is a change in copper concentrations in the brain and central nervous system. Prion protein (PrP) is a copper-binding,...	nmrlearner	Journal club	0	02-26-2013 06:35 PM
NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine. NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine. NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine. Chem Commun (Camb). 2011 Jun 14;47(22):6407-9 Authors: Shoshan MS, Shalev DE, Adriaens W, Merkx M, Hackeng TM, Tshuva EY Abstract The first NMR structure of a Cu(I)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH ~3.0 and ~6.8 Cu(I) binds through one Cys and the Met...	nmrlearner	Journal club	0	09-21-2011 03:31 PM
Toward the Molecular Basis of Inherited Prion Diseases: NMR Structure of the Human Prion Protein with V210I Mutation. Toward the Molecular Basis of Inherited Prion Diseases: NMR Structure of the Human Prion Protein with V210I Mutation. Toward the Molecular Basis of Inherited Prion Diseases: NMR Structure of the Human Prion Protein with V210I Mutation. J Mol Biol. 2011 Aug 4; Authors: Biljan I, Ilc G, Giachin G, Raspadori A, Zhukov I, Plavec J, Legname G The development of transmissible spongiform encephalopathies (TSEs) is associated with the conversion of the cellular prion protein (PrP(C)) into a misfolded, pathogenic isoform (PrP(Sc)). Spontaneous generation...	nmrlearner	Journal club	0	08-16-2011 01:19 PM
[NMR paper] Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II), Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II), and zinc(II): NMR and EPR studies. Related Articles Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II), and zinc(II): NMR and EPR studies. J Am Chem Soc. 2005 Jan 26;127(3):996-1006 Authors: Gaggelli E, Bernardi F, Molteni E, Pogni R, Valensin D, Valensin G, Remelli M, Luczkowski M, Kozlowski H The synthetic peptide encompassing residues 106-126 (PrP106-126, KTNMKHMAGAAAAGAVVGGLG) of the human prion protein was considered for...	nmrlearner	Journal club	0	11-24-2010 11:14 PM
[NMR paper] CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process. Related Articles CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process. J Biol Chem. 2003 Dec 12;278(50):50175-81 Authors: Ziegler J, Sticht H, Marx UC, Müller W, Rösch P, Schwarzinger S The conversion of prion helix 1 from an alpha-helical into an extended conformation is generally assumed to be an essential step in the conversion of the cellular isoform...	nmrlearner	Journal club	0	11-24-2010 09:16 PM
[NMR paper] Prion protein NMR structure and species barrier for prion diseases. Prion protein NMR structure and species barrier for prion diseases. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Prion protein NMR structure and species barrier for prion diseases. Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7281-5 Authors: Billeter M, Riek R, Wider G, Hornemann S, Glockshuber R, WÃ¼thrich K The structural...	nmrlearner	Journal club	0	08-22-2010 05:08 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off