Protein glycosylation is important in many organisms for proper protein folding, signaling, cell adhesion, protein-protein interactions, and immune responses. Thus, effectively determining the extent of glycosylation in glycoprotein therapeutics is crucial. Up to now, characterizing protein glycosylation has been carried out mostly by liquid chromatography mass spectrometry (LC-MS), which requires careful sample processing, e.g., glycan removal or protein digestion and glycopeptide enrichment....
[NMR paper] Detecting aspartate isomerization and backbone cleavage after aspartate in intact proteins by NMR spectroscopy.
Detecting aspartate isomerization and backbone cleavage after aspartate in intact proteins by NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Detecting aspartate isomerization and backbone cleavage after aspartate in intact proteins by NMR spectroscopy.
J Biomol NMR. 2021 Jan 21;:
Authors: Hinterholzer A, Stanojlovic V, Regl C, Huber CG, Cabrele C, Schubert M
Abstract
The monitoring of non-enzymatic...
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Detecting aspartate isomerization and backbone cleavage after aspartate in intact proteins by NMR spectroscopy
Detecting aspartate isomerization and backbone cleavage after aspartate in intact proteins by NMR spectroscopy
Abstract
The monitoring of non-enzymatic post-translational modifications (PTMs) in therapeutic proteins is important to ensure drug safety and efficacy. Together with methionine and asparagine, aspartic acid (Asp) is very sensitive to spontaneous alterations. In particular, Asp residues can undergo isomerization and peptide-bond hydrolysis, especially when embedded in sequence motifs that are prone to succinimide formation or when followed...
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[NMR paper] GPCR Activation States Induced by Nanobodies and Mini-G Proteins Compared by NMR Spectroscopy.
GPCR Activation States Induced by Nanobodies and Mini-G Proteins Compared by NMR Spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.png Related Articles GPCR Activation States Induced by Nanobodies and Mini-G Proteins Compared by NMR Spectroscopy.
Molecules. 2020 Dec 17;25(24):
Authors: Rößler P, Mayer D, Tsai CJ, Veprintsev DB, Schertler GFX, Gossert AD
Abstract
In this work, we examine methyl nuclear magnetic resonance (NMR) spectra of the...
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[ASAP] Glycosylation Fosters Interactions between Model Sea Urchin Spicule Matrix Proteins. Implications for Embryonic Spiculogenesis and Biomineralization
Glycosylation Fosters Interactions between Model Sea Urchin Spicule Matrix Proteins. Implications for Embryonic Spiculogenesis and Biomineralization
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00207/20180517/images/medium/bi-2018-00207u_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00207
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[NMR paper] Probing the Conformationally Excited States of Membrane Proteins via (1)H-detected MAS Solid-State NMR Spectroscopy.
Probing the Conformationally Excited States of Membrane Proteins via (1)H-detected MAS Solid-State NMR Spectroscopy.
Probing the Conformationally Excited States of Membrane Proteins via (1)H-detected MAS Solid-State NMR Spectroscopy.
J Phys Chem B. 2017 Apr 13;:
Authors: Gopinath T, Nelson SE, Soller KJ, Veglia G
Abstract
Proteins exist in ensembles of conformational states that interconvert on various motional time scales. High-energy states of proteins, often referred to as conformationally excited states, are sparsely...
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04-14-2017 10:27 AM
[NMR paper] Posttranslational Modifications of Intact Proteins Detected by NMR Spectroscopy: Application to Glycosylation.
Posttranslational Modifications of Intact Proteins Detected by NMR Spectroscopy: Application to Glycosylation.
Related Articles Posttranslational 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...
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05-01-2015 01:34 PM
[NMR paper] Probing Transient Conformational States of Proteins by Solid-State R1? Relaxation-Dispersion NMR Spectroscopy.
Probing Transient Conformational States of Proteins by Solid-State R1? Relaxation-Dispersion NMR Spectroscopy.
Related Articles Probing Transient Conformational States of Proteins by Solid-State R1? Relaxation-Dispersion NMR Spectroscopy.
Angew Chem Int Ed Engl. 2014 Mar 18;
Authors: Ma P, Haller JD, Zajakala J, Macek P, Sivertsen AC, Willbold D, Boisbouvier J, Schanda P
Abstract
The function of proteins depends on their ability to sample a variety of states differing in structure and free energy. Deciphering how the various thermally...
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03-20-2014 12:44 PM
[NMR paper] Studying excited states of proteins by NMR spectroscopy.
Studying excited states of proteins by NMR spectroscopy.
Related Articles Studying excited states of proteins by NMR spectroscopy.
Nat Struct Biol. 2001 Nov;8(11):932-5
Authors: Mulder FA, Mittermaier A, Hon B, Dahlquist FW, Kay LE
Protein structure is inherently dynamic, with function often predicated on excursions from low to higher energy conformations. For example, X-ray studies of a cavity mutant of T4 lysozyme, L99A, show that the cavity is sterically inaccessible to ligand, yet the protein is able to bind substituted benzenes rapidly....
Glycosylation States on Intact Proteins Determined by NMR Spectroscopy
Linear Mode
