NMR paper Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.

		BioNMR > Educational resources > Journal club
[NMR paper] Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.

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:

View First Unread

Thread Tools

Search this Thread

Rate Thread

Display Modes

02-18-2021, 03:17 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,178

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

Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.

Related Articles Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.

Biomol NMR Assign. 2021 Feb 15;:

Authors: Sanz-Hernández M, De Simone A

Abstract
Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative disorders associated with the misfolding and aggregation of the human prion protein (huPrP). Despite efforts into investigating the process of huPrP aggregation, the mechanisms triggering its misfolding remain elusive. A number of TSE-associated mutations of huPrP have been identified, but their role at the onset and progression of prion diseases is unclear. Here we report the NMR assignments of the C-terminal globular domain of the wild type huPrP and the pathological mutant T183A. The differences in chemical shifts between the two variants reveal conformational alterations in*some structural elements of the mutant, whereas*the analyses of secondary shifts and random coil index provide indications on the putative mechanisms of misfolding of T183A huPrP.

PMID: 33590433 [PubMed - as supplied by publisher]

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] NMR assignments for the C-terminal domain of human TDP-43. NMR assignments for the C-terminal domain of human TDP-43. Related Articles NMR assignments for the C-terminal domain of human TDP-43. Biomol NMR Assign. 2021 Jan 08;: Authors: Pantoja-Uceda D, Stuani C, Laurents DV, McDermott AE, Buratti E, Mompeán M Abstract Transactive response DNA-binding protein of 43*kDa (TDP-43) is a 414-residue protein whose aberrant aggregation is implicated in neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) or frontotemporal lobar degeneration (FTLD). Intriguingly, TDP-43 has...	nmrlearner	Journal club	0	01-10-2021 07:26 PM
[NMR paper] NMR assignments of the C-terminal domain of human galectin-8. NMR assignments of the C-terminal domain of human galectin-8. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR assignments of the C-terminal domain of human galectin-8. Biomol NMR Assign. 2015 Oct;9(2):427-30 Authors: Liu CH, Chien CT, Lin CH, Hsu ST Abstract Galectins recognize ?-galectosides to promote a variety of cellular functions. Despite their sequence variations, all galectins share the same carbohydrate recognition...	nmrlearner	Journal club	0	06-21-2016 01:30 PM
[NMR paper] Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA. Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA. Related Articles Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA. Biomol NMR Assign. 2014 Feb 4; Authors: Jean NL, Bougault C, Derouaux A, Callens G, Vollmer W, Simorre JP Abstract The peptidoglycan is a major component of the bacterial cell wall and is essential to maintain cellular integrity and cell shape. Penicillin-Binding Proteins (PBPs) catalyze the final...	nmrlearner	Journal club	0	02-05-2014 06:08 PM
[NMR paper] Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28. Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28. Related Articles Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28. Biomol NMR Assign. 2013 Dec 24; Authors: Peterson TA, Yu L, Piper RC Abstract Vps28 is one of four cytosolic proteins comprising the endosomal sorting complex required for transport I (ESCRT-I). ESCRT-I is involved in sorting ubiquitinated proteins to multivesicular bodies as well as in mediating budding of retroviruses. Here, we report the backbone...	nmrlearner	Journal club	0	12-25-2013 03:39 PM
[NMR paper] Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis. Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis. Related Articles Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis. Biomol NMR Assign. 2013 Dec 24; Authors: Castellen P, Sforça ML, Gueiros-Filho FJ, de Mattos Zeri AC Abstract Bacterial cell division proteins must assemble at the middle of the cell to ensure the viability of both daughter cells. The first step in the assembly of the...	nmrlearner	Journal club	0	12-25-2013 03:39 PM
Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion Abstract We present the de novo resonance assignments for the crystalline 33 kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly 13C, 15N labeled protein sample, sequential chemical-shift information for 74% of the N, CÎ±, CÎ² triples, and for 80% of further side-chain resonances for these spin systems. We describe the procedures and protocols devised, and discuss possibilities and limitations of the...	nmrlearner	Journal club	0	08-04-2011 01:14 AM
Extensive de novo solid-state NMR assignments of the 33kDa C-terminal domain of the Ure2 prion. Extensive de novo solid-state NMR assignments of the 33kDa C-terminal domain of the Ure2 prion. Extensive de novo solid-state NMR assignments of the 33kDa C-terminal domain of the Ure2 prion. J Biomol NMR. 2011 Jul 31; Authors: Habenstein B, Wasmer C, Bousset L, Sourigues Y, Schütz A, Loquet A, Meier BH, Melki R, Böckmann A We present the de novo resonance assignments for the crystalline 33kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly (13)C, (15)N labeled...	nmrlearner	Journal club	0	08-02-2011 11:40 AM
[NMR paper] Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in fold Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. Related Articles Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J Biomol NMR. 1994 Nov;4(6):845-58 Authors: Zhang O, Kay LE, Olivier JP, Forman-Kay JD The backbone 1H and 15N resonances of the N-terminal SH3 domain of the Drosophila signaling adapter...	nmrlearner	Journal club	0	08-22-2010 03:29 AM

« 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