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...
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07-12-2011 06:23 PM
Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach.
Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach.
Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach.
Curr Protein Pept Sci. 2011 Feb 24;
Authors: Orcellet ML, Fernández CO
The misfolding of proteins into a toxic conformation is proposed to be at the molecular foundation of a number of neurodegenerative disorders including Alzheimer's and Parkinson's diseases. Evidence that ?-synuclein amyloidogenesis plays a causative role in the development of Parkinson's disease is furnished by a...
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02-26-2011 11:56 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
Abstract It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all detectable species. The analysis was carried out using experimental data obtained during aggregation of the 10.4 kDa Crh protein, which has been shown to involve a partially unfolded intermediate...
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01-27-2011 04:31 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
J Biomol NMR. 2011 Jan 21;
Authors: Etzkorn M, Böckmann A, Baldus M
It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all...
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01-22-2011 01:52 PM
Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy.
Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy.
Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy.
J Am Chem Soc. 2010 Dec 15;
Authors: Binolfi A, Valiente-Gabioud AA, Duran R, Zweckstetter M, Griesinger C, Fernandez CO
The aggregation of ?-synuclein (AS) is selectively enhanced by copper in vitro, and the interaction is proposed to play a potential role in vivo. In this work, we report the structural, residue-specific characterization of Cu(I) binding to AS and demonstrate...
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12-17-2010 11:23 AM
[NMR paper] NMR conformational studies of micelle-bound orexin-B: a neuropeptide involved in the
NMR conformational studies of micelle-bound orexin-B: a neuropeptide involved in the sleep/awake cycle and feeding regulation.
Related Articles NMR conformational studies of micelle-bound orexin-B: a neuropeptide involved in the sleep/awake cycle and feeding regulation.
J Biomol Struct Dyn. 2003 Dec;21(3):341-51
Authors: Miskolzie M, Lucyk S, Kotovych G
The preferred conformation of orexin-B, an orphan G-protein coupled receptor agonist (the human sequence is RSGPPGLQGRLQRLLQASGNHAAGILTM-NH(2)) has been determined by (1)H and (13)C 2D NMR...
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11-24-2010 09:16 PM
[NMR paper] Micelle-bound conformation of a hairpin-forming peptide: combined NMR and molecular d
Micelle-bound conformation of a hairpin-forming peptide: combined NMR and molecular dynamics study.
Related Articles Micelle-bound conformation of a hairpin-forming peptide: combined NMR and molecular dynamics study.
Biopolymers. 2002 Nov 15;65(4):284-98
Authors: Dixon AM, Venable RM, Pastor RW, Bull TE
A peptide fragment from a protein hairpin turn region was modified by addition of isoleucine residues to both ends to enhance binding to lipid micelles; the resulting peptide (I(1)-I(2)-C(3)-N(4)-N(5)-P(6)-H(7)-I(8)-I(9)) contains the core...
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11-24-2010 08:58 PM
[NMR paper] 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle.
2D NMR and structural model for a mitochondrial signal peptide bound to a micelle.
Related Articles 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle.
Biochemistry. 1990 Oct 23;29(42):9872-8
Authors: Karslake C, Piotto ME, Pak YK, Weiner H, Gorenstein DG
The 19 amino acid signal peptide of rat liver aldehyde dehydrogenase, possessing a lysine substitution for an arginine and containing 3 extra amino acid residues at the C terminus, was studied by two-dimensional NMR in a dodecylphosphocholine micelle. In this...
Probing the micelle-bound aggregation-prone state of ?-synuclein with (19)F NMR spectroscopy.
Linear Mode
