[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.
Related ArticlesDistinct 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
Abstract
Polyalanine (polyA) sequences are well known as the simplest sequence that naturally forms anti-parallel ?-sheets and constitute a key element in the structure of spider and wild silkworm silk fibers. We have carried out a systematic analysis of the packing of anti-parallel ?-sheets for (Ala)n, n = 5, 6, 7 and 12, using primarily 13C solid-state NMR and MD simulation. HFIP and TFA are frequently used as the dope solvents for recombinant silks, and polyA was solidified from both HFIP and TFA solutions by drying. An analysis of Ala C? peaks in the 13C CP/MAS NMR spectra indicated that polyA from HFIP was mainly rectangular but polyA from TFA was mainly staggered. The transition from the rectangular to the staggered arrangement in (Ala)6 was observed for the first time from the change in the Ala C? peak through heat treatment at 200 °C for 4 h. The removal of the bound water was confirmed by thermal analysis. This transition could be reproduced by MD simulation of (Ala)6 molecules at 200 °C after removal of the bound water molecules. In this way, the origin of the stability of the different packing arrangements of polyA was clarified.
[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] 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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?-Sheet Coreof Tau Paired Helical FilamentsRevealed by Solid-State NMR
?-Sheet Coreof Tau Paired Helical FilamentsRevealed by Solid-State NMR
Venita Daebel, Subashchandrabose Chinnathambi, Jacek Biernat, Martin Schwalbe, Birgit Habenstein, Antoine Loquet, Elias Akoury, Katharina Tepper, Henrik Mu?ller, Marc Baldus, Christian Griesinger, Markus Zweckstetter, Eckhard Mandelkow, Vinesh Vijayan and Adam Lange
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja305470p/aop/images/medium/ja-2012-05470p_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja305470p...
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Packing Interactions inHydrated and Anhydrous Formsof the Antibiotic Ciprofloxacin: a Solid-State NMR, X-ray Diffraction,and Computer Simulation Study
Packing Interactions inHydrated and Anhydrous Formsof the Antibiotic Ciprofloxacin: a Solid-State NMR, X-ray Diffraction,and Computer Simulation Study
Lui?s Mafra, Se?rgio M. Santos, Rene?e Siegel, Ine?s Alves, Filipe A. Almeida Paz, Dmytro Dudenko and Hans W. Spiess
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja208647n/aop/images/medium/ja-2011-08647n_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja208647n
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
Chemistry. 2011 Feb 1;17(5):1547-1560
Authors: Enríquez-Navas PM, Marradi M, Padro D, Angulo J, Penadés S
The structural and affinity details of the interactions of synthetic oligomannosides, linear (di-, tri-, and tetra-) and branched (penta- and hepta-),...
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A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
Chemistry. 2011 Jan 5;
Authors: Enríquez-Navas PM, Marradi M, Padro D, Angulo J, Penadés S
The structural and affinity details of the interactions of synthetic oligomannosides, linear (di-, tri-, and tetra-) and branched (penta- and hepta-), with the broadly...
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[NMR paper] Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR.
Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR.
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J Am Chem Soc. 2005 Sep 7;127(35):12263-72
Authors: Vogel A, Katzka CP, Waldmann H, Arnold K, Brown MF, Huster D
The human N-ras protein binds to cellular membranes by insertion of two covalently bound posttranslational lipid modifications, which is crucial for its...
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[NMR paper] 1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conf
1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conformation changes in horse cytochrome c.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conformation changes in horse cytochrome c.
Eur J Biochem. 1993 Feb 1;211(3):555-62
Authors: Turner DL, Williams RJ
The redox-state dependent changes in chemical shift, which have...
Distinct solvent- and temperature-dependent packing arrangements of anti-parallel ?-sheet polyalanines studied with solid-state 13C NMR and MD simulation.
Linear Mode
