Related ArticlesSolid-state NMR sequential assignment of an Amyloid-?(1-42) fibril polymorph.
Biomol NMR Assign. 2016 May 10;
Authors: Ravotti F, Wälti MA, Güntert P, Riek R, Böckmann A, Meier BH
Abstract
The formation of fibrils of the amyloid-? (A?) peptide is considered to be a key event in the pathology of Alzheimer's disease (AD). The determination of a high-resolution structure of these fibrils is relevant for the understanding of the molecular basis of AD. In this work, we present the sequential resonance assignment of one of the polymorphs of A?(1-42) fibrils. We show that most of the protein is rigid, while a stretch of 4 residues (11-14) is not visible by solid-state NMR spectroscopy due to dynamics.
PMID: 27165577 [PubMed - as supplied by publisher]
[NMR paper] Further exploration of the conformational space of ?-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph.
Further exploration of the conformational space of ?-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph.
Related Articles Further exploration of the conformational space of ?-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph.
Biomol NMR Assign. 2015 Aug 30;
Authors: Verasdonck J, Bousset L, Gath J, Melki R, Böckmann A, Meier BH
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...
nmrlearner
Journal club
0
09-01-2015 10:48 AM
[NMR paper] Nano-mole scale sequential signal assignment by (1)H-detected protein solid-state NMR.
Nano-mole scale sequential signal assignment by (1)H-detected protein solid-state NMR.
Related Articles Nano-mole scale sequential signal assignment by (1)H-detected protein solid-state NMR.
Chem Commun (Camb). 2015 Aug 28;
Authors: Wang S, Parthasarathy S, Xiao Y, Nishiyama Y, Long F, Matsuda I, Endo Y, Nemoto T, Yamauchi K, Asakura T, Takeda M, Terauchi T, Kainosho M, Ishii Y
Abstract
We present a 3D (1)H-detected solid-state NMR (SSNMR) approach for main-chain signal assignments of 10-100 nmol of fully protonated proteins...
nmrlearner
Journal club
0
09-01-2015 10:48 AM
[NMR paper] Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples.
Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples.
Related Articles Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples.
J Biomol NMR. 2015 Mar 7;
Authors: Gopinath T, Mote KR, Veglia G
Abstract
We present a new method called DAISY (Dual Acquisition orIented ssNMR spectroScopY) for the simultaneous acquisition of 2D and 3D oriented solid-state NMR experiments for membrane...
nmrlearner
Journal club
0
03-10-2015 07:22 PM
[NMR paper] Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.
Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.
Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.
Biomol NMR Assign. 2013 Aug 14;
Authors: Schütz AK, Habenstein B, Luckgei N, Bousset L, Sourigues Y, Nielsen AB, Melki R, Böckmann A, Meier BH
Abstract
Sup35p is a yeast prion and is responsible for the trait in Saccharomyces cerevisiae. With 685 amino acids, full-length soluble and fibrillar Sup35p are challenging targets for structural biology as they cannot be investigated...
nmrlearner
Journal club
0
08-15-2013 07:45 PM
[NMR paper] Solid-state NMR sequential assignments of the amyloid core of Sup35pNM.
Solid-state NMR sequential assignments of the amyloid core of Sup35pNM.
Solid-state NMR sequential assignments of the amyloid core of Sup35pNM.
Biomol NMR Assign. 2013 Aug 10;
Authors: Luckgei N, Schütz AK, Habenstein B, Bousset L, Sourigues Y, Melki R, Meier BH, Böckmann A
Abstract
Sup35pNM represents the N-terminal and middle (M) domains of the yeast Saccharomyces cerevisiae prion Sup35p. This fragment is commonly used for structural and functional studies of Sup35p. We here present a solid-state NMR study of fibrils formed by this...
nmrlearner
Journal club
0
08-13-2013 04:26 PM
Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Magn Reson Chem. 2011 Feb;49(2):65-9
Authors: Middleton DA
Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the...
nmrlearner
Journal club
0
01-22-2011 01:52 PM
Solid-State NMR Studies of Amyloid Fibril Structure.
Solid-State NMR Studies of Amyloid Fibril Structure.
Solid-State NMR Studies of Amyloid Fibril Structure.
Annu Rev Phys Chem. 2010 Apr 2;
Authors: Tycko R
Current interest in amyloid fibrils stems from their involvement in neurodegenerative and other diseases and from their role as an alternative structural state for many peptides and proteins. Solid-state nuclear magnetic resonance (NMR) methods have the unique capability of providing detailed structural constraints for amyloid fibrils, sufficient for the development of full molecular models. In...
nmrlearner
Journal club
0
01-12-2011 11:11 AM
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Magn Reson Chem. 2011 Jan 3;
Authors: Middleton DA
Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the secondary...
Solid-state NMR sequential assignment of an Amyloid-?(1-42) fibril polymorph.
Linear Mode
