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 structural component of the Lewy bodies observed in diseased brain. We here present the solid-state NMR sequential assignments of a new fibrillar form of this protein, the first one with a well-ordered and rigid N-terminal part.
PMID: 21744165 [PubMed - as supplied by publisher]
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Abstract Oriented solid-state NMR is the most direct methodology to obtain the orientation of membrane proteins with respect to the lipid bilayer. The method consists of measuring 1H-15N dipolar couplings (DC) and 15N anisotropic chemical shifts (CSA) for membrane proteins that are uniformly aligned with respect to the membrane bilayer. A significant advantage of this approach is that tilt and azimuthal...
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10-10-2011 06:27 AM
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, Cα, Cβ 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...
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08-04-2011 01:14 AM
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.
Extensive de novo solid-state NMR assignments of the 33*kDa 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 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 (13)C, (15)N labeled...
[NMR paper] Solid state NMR sequential resonance assignments and conformational analysis of the 2
Solid state NMR sequential resonance assignments and conformational analysis of the 2x10.4 kDa dimeric form of the Bacillus subtilis protein Crh.
Related Articles Solid state NMR sequential resonance assignments and conformational analysis of the 2x10.4 kDa dimeric form of the Bacillus subtilis protein Crh.
J Biomol NMR. 2003 Dec;27(4):323-39
Authors: Böckmann A, Lange A, Galinier A, Luca S, Giraud N, Juy M, Heise H, Montserret R, Penin F, Baldus M
Solid state NMR sample preparation and resonance assignments of the U- 2x10.4 kDa dimeric form...
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11-24-2010 09:16 PM
[NMR paper] Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state.
Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state.
Related Articles Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state.
J Biomol NMR. 2000 Mar;16(3):209-19
Authors: McDermott A, Polenova T, Bockmann A, Zilm KW, Paulson EK, Martin RW, Montelione GT, Paulsen EK
We demonstrate that high-resolution multidimensional solid state NMR methods can be used to correlate many backbone and side chain chemical shifts for hydrated micro-crystalline U-13C,15N Basic Pancreatic Trypsin Inhibitor...
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11-18-2010 09:15 PM
[NMR paper] Prospects for resonance assignments in multidimensional solid-state NMR spectra of un
Prospects for resonance assignments in multidimensional solid-state NMR spectra of uniformly labeled proteins.
Related Articles Prospects for resonance assignments in multidimensional solid-state NMR spectra of uniformly labeled proteins.
J Biomol NMR. 1996 Oct;8(3):239-51
Authors: Tycko R
The feasibility of assigning the backbone 15N and 13C NMR chemical shifts in multidimensional magic angle spinning NMR spectra of uniformly isotopically labeled proteins and peptides in unoriented solid samples is assessed by means of numerical simulations....
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08-22-2010 02:20 PM
[NMR paper] Solid-state NMR triple-resonance backbone assignments in a protein.
Solid-state NMR triple-resonance backbone assignments in a protein.
Related Articles Solid-state NMR triple-resonance backbone assignments in a protein.
J Biomol NMR. 1999 Apr;13(4):337-42
Authors: Tan WM, Gu Z, Zeri AC, Opella SJ
Triple-resonance solid-state NMR spectroscopy is demonstrated to sequentially assign the 13C' and 15N amide backbone resonances of adjacent residues in an oriented protein sample. The observed 13C' chemical shift frequency provides an orientational constraint complementary to those measured from the 1H and 15N amide...
Solid-state NMR sequential assignments of ?-synuclein.
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