Chow, Wing Ying, Rui Li, Ieva Goldberga, David G. Reid, Rakesh Rajan, Jonathan Clark, Hartmut Oschkinat, Melinda J. Duer, Robert Hayward, and Catherine M. Shanahan. “Essential but Sparse Collagen Hydroxylysyl Post-Translational Modifications Detected by DNP NMR.” Chemical Communications 54, no. 89 (2018): 12570–73.
The sparse but functionally essential post-translational collagen modification 5-hydroxylysine can undergo further transformations, including crosslinking, O-glycosylation, and glycation. Dynamic nuclear polarization (DNP) and stable isotope enriched lysine incorporation provide sufficient solid-state NMR sensitivity to identify these adducts directly in skin and vascular smooth muscle cell extracellular matrix (ECM), without extraction procedures, by comparison with chemical shifts of model compounds. Thus, DNP provides access to the elucidation of structural consequences of collagen modifications in intact tissue.
[ASAP] Post-Translational Modifications in Polypyrimidine Tract Binding Proteins PTBP1 and PTBP2
Post-Translational Modifications in Polypyrimidine Tract Binding Proteins PTBP1 and PTBP2
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00256/20180613/images/medium/bi-2018-00256v_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00256
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06-14-2018 08:12 AM
Post-Translational Modifications of Protein Backbones:Unique Functions, Mechanisms, and Challenges
Post-Translational Modifications of Protein Backbones:Unique Functions, Mechanisms, and Challenges
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00861/20171103/images/medium/bi-2017-00861b_0001.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00861
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11-04-2017 12:23 PM
[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] Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
Related Articles Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
J Biol Chem. 2013 Jan 22;
Authors: De Sa Peixoto P, Laurent G, Azais T, Mosser G
Abstract
In vivo, collagen I, the major structural protein in human body, is found assembled into fibrils. In the present work, we study a high concentrated collagen sample in its soluble, fibrillar and denatured states...
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02-03-2013 10:19 AM
Cell signaling, post-translational protein modifications and NMR spectroscopy
Cell signaling, post-translational protein modifications and NMR spectroscopy
Abstract Post-translationally modified proteins make up the majority of the proteome and establish, to a large part, the impressive level of functional diversity in higher, multi-cellular organisms. Most eukaryotic post-translational protein modifications (PTMs) denote reversible, covalent additions of small chemical entities such as phosphate-, acyl-, alkyl- and glycosyl-groups onto selected subsets of modifiable amino acids. In turn, these modifications induce highly specific changes in the chemical ...
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09-29-2012 11:56 AM
Postdoctoral Fellow - Post-translational modification, NMR : Duarte ...
Postdoctoral Fellow - Post-translational modification, NMR : Duarte ...
Postdoctoral Fellow - Post-translational modification, NMR, Duarte, United States. View all science jobs and scientific careers from Nature Jobs, the premier ...
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01-10-2012 03:38 PM
[NMR paper] Heteronuclear NMR studies of the specificity of the post-translational modification o
Heteronuclear NMR studies of the specificity of the post-translational modification of biotinyl domains by biotinyl protein ligase.
Related Articles Heteronuclear NMR studies of the specificity of the post-translational modification of biotinyl domains by biotinyl protein ligase.
FEBS Lett. 2000 Aug 18;479(3):93-8
Authors: Reche PA, Howard MJ, Broadhurst RW, Perham RN
The lipoyl domains of 2-oxo acid dehydrogenase multienzyme complexes and the biotinyl domains of biotin-dependent enzymes have homologous structures, but the target lysine...
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11-19-2010 08:29 PM
[NMR paper] Post-translational heterocyclic backbone modifications in the 43-peptide antibiotic m
Post-translational heterocyclic backbone modifications in the 43-peptide antibiotic microcin B17. Structure elucidation and NMR study of a 13C,15N-labelled gyrase inhibitor.
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 Post-translational heterocyclic backbone modifications in the 43-peptide antibiotic microcin B17. Structure elucidation and NMR study of a 13C,15N-labelled gyrase inhibitor.
Eur J Biochem. 1995 Dec 1;234(2):414-26
Authors: ...