Related ArticlesPosttranslational Modifications of Intact Proteins Detected by NMR Spectroscopy: Application to Glycosylation.
Angew Chem Int Ed Engl. 2015 Apr 29;
Authors: Schubert M, Walczak MJ, Aebi M, Wider G
Abstract
Posttranslational modifications (PTMs) are an integral part of the majority of proteins. The characterization of structure and function of PTMs can be very challenging especially for glycans. Existing methods to analyze PTMs require complicated sample preparations and suffer from missing certain modifications, the inability to identify linkage types and thus chemical structure. We present a direct, robust, and simple NMR spectroscopy method for the detection and identification of PTMs in proteins. No isotope labeling is required, nor does the molecular weight of the studied protein limit the application. The method can directly detect modifications on intact proteins without sophisticated sample preparation. This approach is well suited for diagnostics of proteins derived from native organisms and for the quality control of biotechnologically produced therapeutic proteins.
PMID: 25924827 [PubMed - as supplied by publisher]
[NMR paper] Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
Angew Chem Int Ed Engl. 2013 Mar 11;52(11):3145-7
Authors: Werbeck ND, Kirkpatrick J,...
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The application of paramagnetic lanthanoid ions in NMR spectroscopy on proteins
The application of paramagnetic lanthanoid ions in NMR spectroscopy on proteins
Publication date: Available online 4 November 2013
Source:Coordination Chemistry Reviews</br>
Author(s): Wei-Min Liu , Mark Overhand , Marcellus Ubbink</br>
Lanthanoids are gaining popularity as paramagnetic centers for high resolution nuclear magnetic resonance (NMR) spectroscopy. They provide valuable angular and long-distance restraints for structure calculations of proteins and protein complexes. The introduction of lanthanoids into a protein sample is complicated by the many...
[NMR paper] Proton-Detected Solid-State NMR Spectroscopy at Aliphatic Sites: Application to Crystalline Systems.
Proton-Detected Solid-State NMR Spectroscopy at Aliphatic Sites: Application to Crystalline Systems.
Related Articles Proton-Detected Solid-State NMR Spectroscopy at Aliphatic Sites: Application to Crystalline Systems.
Acc Chem Res. 2013 Jun 7;
Authors: Asami S, Reif B
Abstract
When applied to biomolecules, solid-state NMR suffers from low sensitivity and resolution. The major obstacle to applying proton detection in the solid state is the proton dipolar network, and deuteration can help avoid this problem. In the past, researchers...
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Angew Chem Int Ed Engl. 2011 Apr 14;
Authors: Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez Del Amo JM, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B
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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.
Related Articles Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR.
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...
Posttranslational Modifications of Intact Proteins Detected by NMR Spectroscopy: Application to Glycosylation.
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