Related ArticlesParallel ?-Sheet Structure of Alanine Tetrapeptide in the Solid State As Studied by Solid-State NMR Spectroscopy.
J Phys Chem B. 2016 09 01;120(34):8932-41
Authors: Asakura T, Horiguchi K, Aoki A, Tasei Y, Naito A
Abstract
The structural analysis of alanine oligopeptides is important for understanding the crystalline region in silks from spiders and wild silkworms and also the mechanism of cellular toxicity of human diseases arising from expansion in polyalanine sequences. The atomic-level structures of alanine tripeptide and tetrapeptide with antiparallel ?-sheet structures (AP-Ala3 and AP-Ala4, respectively) together with alanine tripeptide with parallel ?-sheet structures (P-Ala3) have been determined, but alanine tetrapeptide with a parallel ?-sheet structure (P-Ala4) has not been reported yet. In this article, first, we established the preparation protocol of P-Ala4 from more stable AP-Ala4. Second, complete assignments of the (13)C, (15)N, and (1)H solid-state NMR spectra were performed with (13)C- and (15)N-labeled Ala4 samples using several solid-state NMR techniques. Then, the structural constraints were obtained, for example, the amide proton peaks of P-Ala4 in the (1)H double-quantum magic-angle spinning NMR spectrum were heavily overlapped and observed at about 7.4 ppm, which was a much higher field than that of 8.7-9.1 ppm observed for AP-Ala4, indicating that the intermolecular hydrogen-bond lengths across strands (N-H···O?C) were considerably longer for P-Ala4, that is, 2.21-2.34 Å, than those reported for AP-Ala4, that is, 1.8-1.9 Å. The structural model was proposed for P-Ala4 by NMR results and MD calculations.
[NMR paper] Distinct solvent- and temperature-dependent packing arrangements of anti-parallel ?-sheet polyalanines studied with solid-state 13C NMR and MD simulation.
Distinct solvent- and temperature-dependent packing arrangements of anti-parallel ?-sheet polyalanines studied with solid-state 13C NMR and MD simulation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Distinct solvent- and temperature-dependent packing arrangements of anti-parallel ?-sheet polyalanines studied with solid-state 13C NMR and MD simulation.
Phys Chem Chem Phys. 2017 Aug 09;19(31):20829-20838
Authors: Kametani S, Tasei Y, Nishimura A, Asakura T
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[NMR paper] Packing Arrangements and Inter-Sheet Interaction of Alanine Oligopeptides as Revealed by Relaxation Parameters Obtained From High-Resolution (13)C Solid-State NMR.
Packing Arrangements and Inter-Sheet Interaction of Alanine Oligopeptides as Revealed by Relaxation Parameters Obtained From High-Resolution (13)C Solid-State NMR.
Related Articles Packing Arrangements and Inter-Sheet Interaction of Alanine Oligopeptides as Revealed by Relaxation Parameters Obtained From High-Resolution (13)C Solid-State NMR.
J Phys Chem B. 2017 Sep 05;:
Authors: Naito A, Tasei Y, Nishimura A, Asakura T
Abstract
Alanine oligopeptides provide a key structure of the crystalline domains of the silks from spiders and...
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[NMR paper] Difference in the structures of alanine tri- and tetra-peptides with antiparallel ?-sheet assessed by X-ray diffraction, solid-state NMR and chemical shift calculations by GIPAW.
Difference in the structures of alanine tri- and tetra-peptides with antiparallel ?-sheet assessed by X-ray diffraction, solid-state NMR and chemical shift calculations by GIPAW.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png Related Articles Difference in the structures of alanine tri- and tetra-peptides with antiparallel ?-sheet assessed by X-ray diffraction, solid-state NMR and chemical shift calculations by GIPAW.
Biopolymers. 2014 Jan;101(1):13-20
Authors: ...
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[NMR paper] Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
Related Articles Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
J Mol Biol. 2013 Nov 15;
Authors: Sackett K, Nethercott MJ, Zheng Z, Weliky DP
Abstract
The HIV gp41 protein catalyzes fusion between viral and target cell membranes. Although...
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Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state
Publication date: Available online 16 November 2013
Source:Journal of Molecular Biology</br>
Author(s): Kelly Sackett , Matthew J. Nethercott , Zhaoxiong Zheng , David P. Weliky</br>
The HIV gp41 protein catalyzes fusion between viral and target cell membranes. Although the ~20-residue N-terminal fusion peptide (FP) region is critical for fusion, the structure of this region is not...
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[NMR paper] Determination of accurate 1H positions of an alanine tripeptide with anti-parallel and parallel ?-sheet structures by high resolution 1H solid state NMR and GIPAW chemical shift calculation.
Determination of accurate 1H positions of an alanine tripeptide with anti-parallel and parallel ?-sheet structures by high resolution 1H solid state NMR and GIPAW chemical shift calculation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Determination of accurate 1H positions of an alanine tripeptide with anti-parallel and parallel ?-sheet structures by high resolution 1H solid state NMR and GIPAW chemical shift calculation.
Chem Commun (Camb). 2012 Nov 25;48(91):11199-201
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[NMR paper] G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
Biochem J. 2013 Mar 15;450(3):443-57
Authors: Ding X, Zhao X, Watts A
Abstract
GPCRs (G-protein-coupled receptors) are versatile signalling molecules at the cell surface and make up the largest and most diverse family of membrane receptors in the human genome. They convert a large variety of extracellular stimuli into...