Abstract
Polymorphism is a common and important phenomenon for protein fibrils which has been linked to the appearance of strains in prion and other neurodegenerative diseases. Parkinson disease is a frequently occurring neurodegenerative pathology, tightly associated with the formation of Lewy bodies. These deposits mainly consist of ?-synuclein in fibrillar, ?-sheet-rich form. ?-synuclein is known to form numerous different polymorphs, which show distinct structural features. Here, we describe the chemical shift assignments, and derive the secondary structure, of a polymorph that was fibrillized at higher-than-physiological pH conditions. The fibrillar core contains residues 40-95, with both the C- and N-terminus not showing any ordered, rigid parts. The chemical shifts are similar to those recorded previously for an assigned polymorph that was fibrillized at neutral pH.
PMID: 26318307 [PubMed - as supplied by publisher]
Solid state NMR chemical shift assignment and conformational analysis of a cellulose binding protein facilitated by optimized glycerol enrichment
Solid state NMR chemical shift assignment and conformational analysis of a cellulose binding protein facilitated by optimized glycerol enrichment
Abstract
Magic-angle spinning solid-state NMR has been applied to study CBM3bâ??Cbh9A (CBM3b), a cellulose binding module protein belonging to family 3b. It is a 146-residue protein having a unique nine-stranded β-sandwich fold, in which 35Â*% of the structure is in a β-sheet conformation and the remainder of the protein is composed of loops and unstructured regions. Yet, the protein can be crystalized...
nmrlearner
Journal club
0
06-19-2014 10:21 PM
[NMR paper] Solid state NMR chemical shift assignment and conformational analysis of a cellulose binding protein facilitated by optimized glycerol enrichment.
Solid state NMR chemical shift assignment and conformational analysis of a cellulose binding protein facilitated by optimized glycerol enrichment.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Solid state NMR chemical shift assignment and conformational analysis of a cellulose binding protein facilitated by optimized glycerol enrichment.
J Biomol NMR. 2014 May 14;
Authors: Ivanir H, Goldbourt A
Abstract
Magic-angle spinning...
nmrlearner
Journal club
0
05-16-2014 08:06 PM
[NMR paper] Solid-State (13)C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein.
Solid-State (13)C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein.
Related Articles Solid-State (13)C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein.
J Mol Biol. 2013 Apr 11;
Authors: Leftin A, Job C, Beyer K, Brown MF
Abstract
Misfolding and aggregation of the intrinsically disordered protein ?-Synuclein (?S) in Lewy body plaques is a characteristic marker of late-stage Parkinson's disease. It is...
nmrlearner
Journal club
0
04-16-2013 07:46 PM
Solid-State 13C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein
Solid-State 13C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein
Publication date: Available online 11 April 2013
Source:Journal of Molecular Biology</br>
Author(s): Avigdor Leftin , Constantin Job , Klaus Beyer , Michael F. Brown</br>
Misfolding and aggregation of the intrinsically disordered protein ?-Synuclein (?S) in Lewy body plaques is a characteristic marker of late-stage Parkinson’s disease. It is well established that membrane binding is initiated at the N-terminus of the protein and...
nmrlearner
Journal club
0
04-11-2013 09:27 PM
Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
J Mol Biol. 2011 Jul 13;
Authors: Schneider R, Schumacher MC, Mueller H, Nand D, Klaukien V, Heise H, Riedel D, Wolf G, Behrmann E, Raunser S, Seidel R, Engelhard M, Baldus M
Protein aggregation via polyglutamine stretches occurs in a number of severe neurodegenerative diseases such as Huntington's disease. We have investigated fibrillar aggregates of polyglutamine peptides...
nmrlearner
Journal club
0
07-19-2011 07:52 PM
Solid-state NMR sequential assignments of ?-synuclein.
Solid-state NMR sequential assignments of ?-synuclein.
Solid-state NMR sequential assignments of ?-synuclein.
Biomol NMR Assign. 2011 Jul 9;
Authors: Gath J, Habenstein B, Bousset L, Melki R, Meier BH, Böckmann A
Parkinson's disease is amongst the most frequent and most devastating neurodegenerative diseases. It is tightly associated with the assembly of proteins into high-molecular weight protein species, which propagate between neurons in the central nervous system. The principal protein involved in this process is ?-synuclein which is a...
nmrlearner
Journal club
0
07-12-2011 06:23 PM
Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.
Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.
Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.
J Mol Biol. 2010 Nov 18;
Authors: Van Melckebeke H, Schanda P, Gath J, Wasmer C, Verel R, Lange A, Meier BH, Böckmann A
Despite its importance in the context of conformational diseases, structural information is still sparse for protein fibrils. Hydrogen/deuterium exchange measurements of backbone amides allow to identify hydrogen-bonding patterns and reveal pertinent information about...
nmrlearner
Journal club
0
11-26-2010 05:32 PM
[NMR paper] High resolution 13C-solid state NMR of bacteriorhodopsin: assignment of specific aspa
High resolution 13C-solid state NMR of bacteriorhodopsin: assignment of specific aspartic acids and structural implications of single site mutations.
Related Articles High resolution 13C-solid state NMR of bacteriorhodopsin: assignment of specific aspartic acids and structural implications of single site mutations.
Eur Biophys J. 1990;18(1):17-24
Authors: Engelhard M, Hess B, Metz G, Kreutz W, Siebert F, Soppa J, Oesterhelt D
Three mutant strains of Halobacterium sp. GRB with the site of mutation in the bacterioopsin gene (PM 326:...
Further exploration of the conformational space of ?-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph.
Linear Mode
