Related ArticlesQuantification of protein secondary structure by (13)C solid-state NMR.
Anal Bioanal Chem. 2016 Apr 11;
Authors: Andrade FD, Forato LA, Bernardes Filho R, Colnago LA
Abstract
High-resolution (13)C solid-state NMR stands out as one of the most promising techniques to solve the structure of insoluble proteins featuring biological and technological importance. The simplest nuclear magnetic resonance (NMR) spectroscopy method to quantify the secondary structure of proteins uses the areas of carbonyl and alpha carbon peaks. The quantification obtained by fitting procedures depends on the assignment of the peaks to the structure, type of line shape, number of peaks to be used, and other parameters that are set by the operator. In this paper, we demonstrate that the analysis of (13)C NMR spectra by a pattern recognition method-based on the singular value decomposition (SVD) regression, which does not depend on the operator-shows higher correlation coefficients for ?-helix and ?-sheet (0.96 and 0.91, respectively) than Fourier transform infrared spectroscopy (FTIR) method. Therefore, the use of (13)C solid-state NMR spectra and SVD is a simple and reliable method for quantifying the secondary structures of insoluble proteins in solid-state.
PMID: 27068694 [PubMed - as supplied by publisher]
[NMR paper] Protein secondary structure of Green Lynx spider dragline silk investigated by solid-state NMR and X-ray diffraction.
Protein secondary structure of Green Lynx spider dragline silk investigated by solid-state NMR and X-ray diffraction.
Related Articles Protein secondary structure of Green Lynx spider dragline silk investigated by solid-state NMR and X-ray diffraction.
Int J Biol Macromol. 2015 Jul 29;
Authors: Xu D, Shi X, Thompson F, Weber WS, Mou Q, Yarger JL
Abstract
In this study, the secondary structure of the major ampullate silk from Peucetia viridans (Green Lynx) spiders is characterized by X-ray diffraction and solid-state NMR...
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Protein Secondary Structure of Green Lynx Spider Dragline Silk Investigated by Solid-state NMR and X-ray Diffraction
Protein Secondary Structure of Green Lynx Spider Dragline Silk Investigated by Solid-state NMR and X-ray Diffraction
Publication date: Available online 29 July 2015
Source:International Journal of Biological Macromolecules</br>
Author(s): Dian Xu, Xiangyan Shi, Forrest Thompson, Warner S. Weber, Qiushi Mou, Jeffery L. Yarger</br>
In this study, the secondary structure of the major ampullate silk from Peucetia viridans (Green Lynx) spiders is characterized by X-ray diffraction and solid-state NMR spectroscopy. From X-ray diffraction measurement, ?-sheet...
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[NMR paper] Characterizing the Secondary Protein Structure of Black Widow Dragline Silk Using Solid-State NMR & X-ray Diffraction.
Characterizing the Secondary Protein Structure of Black Widow Dragline Silk Using Solid-State NMR & X-ray Diffraction.
Characterizing the Secondary Protein Structure of Black Widow Dragline Silk Using Solid-State NMR & X-ray Diffraction.
Biomacromolecules. 2013 Sep 11;
Authors: Sampath S, Jenkins JE, Butler E, Kim J, Henning RW, Holland GP, Yarger JL
Abstract
This study provides a detailed secondary structural characterization of major ampullate dragline silk from Latrodectus hesperus (black widow) spiders. X-ray diffraction results show...
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09-13-2013 12:05 PM
[NMR paper] Solid-state NMR studies of the secondary structure of a mutant prion protein fragment
Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.
Related Articles Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.
Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11686-90
Authors: Laws DD, Bitter HM, Liu K, Ball HL, Kaneko K, Wille H, Cohen FE, Prusiner SB, Pines A, Wemmer DE
The secondary structure of a 55-residue fragment of the mouse prion protein, MoPrP(89-143), was studied in...
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11-19-2010 08:44 PM
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state N
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy
Abstract We present the quantification of backbone amide hydrogen-deuterium exchange rates (HDX) for immobilized proteins. The experiments make use of the deuterium isotope effect on the amide nitrogen chemical shift, as well as on proton dilution by deuteration. We find that backbone amides in the microcrystalline α-spectrin SH3 domain exchange rather slowly with the solvent (with exchange rates negligible within the individual 15Nâ??T 1 timescales). We observed chemical exchange for 6...
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10-27-2010 08:51 AM
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state N
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy.
Related Articles Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy.
J Biomol NMR. 2010 Oct 20;
Authors: Del Amo JM, Fink U, Reif B
We present the quantification of backbone amide hydrogen-deuterium exchange rates (HDX) for immobilized proteins. The experiments make use of the deuterium isotope effect on the amide nitrogen chemical shift, as well as on proton dilution by deuteration. We find that...
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10-22-2010 06:02 AM
[NMR paper] Simple techniques for the quantification of protein secondary structure by 1H NMR spe
Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopy.
FEBS Lett. 1991 Nov 18;293(1-2):72-80
Authors: Wishart DS, Sykes BD, Richards FM
Previous work by Wishart et al. (in press) and others has shown a strong tendency for protein secondary structure to be manifested in 1H NMR chemical...
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08-21-2010 11:12 PM
[NMR paper] Simple techniques for the quantification of protein secondary structure by 1H NMR spe
Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopy.
FEBS Lett. 1991 Nov 18;293(1-2):72-80
Authors: Wishart DS, Sykes BD, Richards FM
Previous work by Wishart et al. (in press) and others has shown a strong tendency for protein secondary structure to be manifested in 1H NMR chemical...
Quantification of protein secondary structure by (13)C solid-state NMR.
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