Ubiquitylation refers to the attachment of mono- or poly-ubiquitin molecules to a substrate protein. To shield ubiquitin chains against potential hydrolysis, a facile, click-chemistry based approach was recently established for the generation of site-specifically conjugated ubiquitin dimers relying on triazole linkage. Here, the preparation of such ubiquitin chains was advanced by the generation of homotypic Lys11-linked ubiquitin trimers considering an isotopic labeling scheme in a moiety-wise...
[NMR paper] NMR Characterization of Conformational Interconversions of Lys48-Linked Ubiquitin Chains.
NMR Characterization of Conformational Interconversions of Lys48-Linked Ubiquitin Chains.
Related Articles NMR Characterization of Conformational Interconversions of Lys48-Linked Ubiquitin Chains.
Int J Mol Sci. 2020 Jul 28;21(15):
Authors: Hiranyakorn M, Yanaka S, Satoh T, Wilasri T, Jityuti B, Yagi-Utsumi M, Kato K
Abstract
Ubiquitin (Ub) molecules can be enzymatically connected through a specific isopeptide linkage, thereby mediating various cellular processes by binding to Ub-interacting proteins through their hydrophobic...
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08-01-2020 02:01 PM
DNP NMR spectroscopy of cross-linked organic polymers: rational guidelines towards optimal sample preparation #DNPNMR
From The DNP-NMR Blog:
DNP NMR spectroscopy of cross-linked organic polymers: rational guidelines towards optimal sample preparation #DNPNMR
Tanaka, Shinji, Wei-Chih Liao, Atsuko Ogawa, Kazuhiko Sato, and Christophe Copéret. “DNP NMR Spectroscopy of Cross-Linked Organic Polymers: Rational Guidelines towards Optimal Sample Preparation.” Physical Chemistry Chemical Physics 22, no. 6 (2020): 3184–90.
https://doi.org/10.1039/C9CP05208A.
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[NMR paper] Structural and Dynamic Characterization of Artificially Linked Ubiquitin Dimers by NMR spectroscopy.
Structural and Dynamic Characterization of Artificially Linked Ubiquitin Dimers by NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png Related Articles Structural and Dynamic Characterization of Artificially Linked Ubiquitin Dimers by NMR spectroscopy.
Chembiochem. 2019 Mar 28;:
Authors: Zhao X, Mißun M, Schneider T, Müller F, Lutz J, Scheffner M, Marx A, Kovermann M
Abstract
As one of the most prevalent post-translational...
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03-30-2019 05:11 AM
Proteomics Finding May Lead to Therapy Targeted at Cellular Pathway Linked to ALS - Genetic Engineering & Biotechnology News
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Proteomics Finding May Lead to Therapy Targeted at Cellular Pathway Linked to ALS
Genetic Engineering & Biotechnology News
Until the publication of this study, several mechanistic details of how the low-complexity domain of hnRNPA2 worked and how it changed into aggregates in disease were unknown, he says. Using nuclear magnetic resonance (NMR) spectroscopy, computer ...
Droplets of...
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01-21-2018 05:03 PM
NMR Structure of the HumanRad18 Zinc Finger in Complexwith Ubiquitin Defines a Class of UBZ Domains in Proteins Linked tothe DNA Damage Response
NMR Structure of the HumanRad18 Zinc Finger in Complexwith Ubiquitin Defines a Class of UBZ Domains in Proteins Linked tothe DNA Damage Response
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi500823h/20140915/images/medium/bi-2014-00823h_0006.gif
Biochemistry
DOI: 10.1021/bi500823h
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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09-15-2014 07:13 PM
[NMR paper] NMR structure of the human Rad18 zinc finger in complex with ubiquitin defines a class of UBZ domains in proteins linked to the DNA damage response.
NMR structure of the human Rad18 zinc finger in complex with ubiquitin defines a class of UBZ domains in proteins linked to the DNA damage response.
NMR structure of the human Rad18 zinc finger in complex with ubiquitin defines a class of UBZ domains in proteins linked to the DNA damage response.
Biochemistry. 2014 Aug 27;
Authors: Rizzo AA, Salerno PE, Bezsonova I, Korzhnev DM
Abstract
Ubiquitin-mediated interactions are critical for the cellular DNA damage response (DDR). Therefore, many DDR-related proteins contain...
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08-28-2014 10:09 AM
NMR analysis of Lys63-linked polyubiquitin recognition by the tandem ubiquitin-interacting motifs of Rap80
NMR analysis of Lys63-linked polyubiquitin recognition by the tandem ubiquitin-interacting motifs of Rap80
Abstract Ubiquitin is a post-translational modifier that is involved in cellular functions through its covalent attachment to target proteins. Ubiquitin can also be conjugated to itself at seven lysine residues and at its amino terminus to form eight linkage-specific polyubiquitin chains for individual cellular processes. The Lys63-linked polyubiquitin chain is recognized by tandem ubiquitin-interacting motifs (tUIMs) of Rap80 for the regulation of DNA repair. To understand the...
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02-25-2012 12:16 AM
[NMR paper] Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Related Articles Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Proteins. 2005 Aug 15;60(3):367-81
Authors: van Dijk AD, Fushman D, Bonvin AM
When classical, Nuclear Overhauser Effect (NOE)-based approaches fail, it is possible, given high-resolution...