Related ArticlesNMR of glycoproteins: profiling, structure, conformation and interactions.
Curr Opin Struct Biol. 2020 Oct 28;68:9-17
Authors: Unione L, Ardá A, Jiménez-Barbero J, Millet O
Abstract
In glycoproteins, carbohydrates are responsible for the selective interaction and tight regulation of cellular processes, constituting the main information transducer interface in protein-glycoprotein interactions. Increasing experimental and computational evidence suggest that such interactions often induce allosteric changes in the host protein, underlining the importance of studying intact glycoproteins. Technical issues have precluded such studies for years but, nowadays, a promising era is emerging where NMR spectroscopy, among other techniques, allows the characterization of the composition, structure and segmental dynamics of glycoproteins. In this review, we discuss such advances and highlight some selected examples. This novel technology unravels multiple new functional mechanisms, subtly hidden within the sugar code.
PMID: 33129067 [PubMed - as supplied by publisher]
[NMR paper] Sparse isotope labeling for nuclear magnetic resonance (NMR) of glycoproteins using 13C-glucose.
Sparse isotope labeling for nuclear magnetic resonance (NMR) of glycoproteins using 13C-glucose.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--academic.oup.com-images-oup_pubmed.png Related Articles Sparse isotope labeling for nuclear magnetic resonance (NMR) of glycoproteins using 13C-glucose.
Glycobiology. 2020 Sep 08;:
Authors: Rogals MJ, Yang JY, Williams RV, Moremen KW, Amster IJ, Prestegard JH
Abstract
Preparation of samples for nuclear magnetic resonance (NMR) characterization of larger proteins...
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09-13-2020 09:18 AM
[NMR paper] NMR Resonance Assignment Methodology: Characterizing Large Sparsely Labeled Glycoproteins.
NMR Resonance Assignment Methodology: Characterizing Large Sparsely Labeled Glycoproteins.
Related Articles NMR Resonance Assignment Methodology: Characterizing Large Sparsely Labeled Glycoproteins.
J Mol Biol. 2019 Apr 26;:
Authors: Chalmers GR, Eletsky A, Morris LC, Yang JY, Tian F, Woods RJ, Moremen KW, Prestegard JH
Abstract
Characterization of proteins using NMR methods begins with assignment of resonances to specific residues. This is usually accomplished using sequential connectivities between nuclear pairs in proteins...
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04-30-2019 03:58 PM
NMR detection and characterization of sialylated glycoproteins and cell surface polysaccharides
NMR detection and characterization of sialylated glycoproteins and cell surface polysaccharides
Abstract Few solution NMR pulse sequences exist that are explicitly designed to characterize carbohydrates (glycans). This is despite the essential role carbohydrate motifs play in cellâ??cell communication, microbial pathogenesis, autoimmune disease progression and cancer metastasis, and despite that fact that glycans, often shed to extra-cellular fluids, can be diagnostic of disease. Here we present a suite of two dimensional coherence experiments to measure three different correlations...
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09-30-2011 08:01 PM
[NMR paper] NMR studies of restriction enzyme-DNA interactions: role of conformation in sequence
NMR studies of restriction enzyme-DNA interactions: role of conformation in sequence specificity.
Related Articles NMR studies of restriction enzyme-DNA interactions: role of conformation in sequence specificity.
Biochemistry. 2005 Apr 5;44(13):5065-74
Authors: Dupureur CM
Sequence specific DNA binding proteins are thought to adopt distinct conformations when binding to target (cognate) and nontarget (noncognate) sequences. There is both biochemical and crystallographic evidence that this behavior is important in mediating sequence recognition...
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11-25-2010 08:21 PM
Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a m
Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system.
Related Articles Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system.
Prog Nucl Magn Reson Spectrosc. 2010 May;56(4):346-59
Authors: Kato K, Yamaguchi Y, Arata Y
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[NMR paper] NMR studies of retinoid-protein interactions: the conformation of [13C]-beta-ionones
NMR studies of retinoid-protein interactions: the conformation of -beta-ionones bound to beta-lactoglobulin B.
Related Articles NMR studies of retinoid-protein interactions: the conformation of -beta-ionones bound to beta-lactoglobulin B.
Pharm Res. 1999 May;16(5):651-9
Authors: Curley RW, Sundaram AK, Fowble JW, Abildgaard F, Westler WM, Markley JL
PURPOSE: Vitamin A (retinol) and its metabolites comprise the natural retinoids. While the biological action of these molecules are thought to be primarily mediated by ca. 55 kDa nuclear retinoic...
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08-21-2010 04:03 PM
Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a m
Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 19 March 2010</br>
Koichi, Kato , Yoshiki, Yamaguchi , Yoji, Arata</br>
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08-16-2010 03:50 AM
Enhanced production and isotope enrichment of recombinant glycoproteins produced in c
Abstract NMR studies of post-translationally modified proteins are complicated by the lack of an efficient method to produce isotope enriched recombinant proteins in cultured mammalian cells. We show that reducing the glucose concentration and substituting glutamate for glutamine in serum-free medium increased cell viability while simultaneously increasing recombinant protein yield and the enrichment of non-essential amino acids compared to culture in unmodified, serum-free medium. Adding dichloroacetate, a pyruvate dehydrogenase kinase inhibitor, further improves cell viability, recombinant...
NMR of glycoproteins: profiling, structure, conformation and interactions.
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