Current chemistries to prepare Adenosine Diphosphate ribosylated (ADPr) peptides are not generally applicable due to the labile nature of this post-translational modification and its incompatibility with strong acidic conditions used in standard solid phase peptide synthesis protocols. We present a general strategy to prepare ADPr peptide analogues based on a copper catalysed click reaction between an azide modified peptide and an alkyne modified ADPr counterpart. We expand the scope of this approach to proteins by preparing two ADPr Ubiquitin analogues carrying the biological relevant ?-glycosidic linkage. Biochemical validation using Legionella effector enzyme SdeA shows that clicked Ub-ADPr is well tolerated and highlights the potential of this strategy to prepare ADPr proteins.
This Is The Closest Look We've Ever Had at The Proteins Linked to Alzheimer's Disease - ScienceAlert
This Is The Closest Look We've Ever Had at The Proteins Linked to Alzheimer's Disease - ScienceAlert
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This Is The Closest Look We've Ever Had at The Proteins Linked to Alzheimer's Disease
ScienceAlert
Extra readings from solid-state nuclear magnetic resonance (NMR) spectroscopy and X-ray diffraction experiments helped to validate the data and the atomic structure, producing a computer rendering that's the most...
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09-12-2017 01:45 PM
A General Mechanism for the Propagation of MutationalEffects in Proteins
A General Mechanism for the Propagation of MutationalEffects in Proteins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00798/20161227/images/medium/bi-2016-00798h_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00798
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12-28-2016 04:14 PM
[NMR paper] Insight to the binding mode of triazole RGD-peptidomimetics to integrin-rich cancer cells by NMR and molecular modeling.
Insight to the binding mode of triazole RGD-peptidomimetics to integrin-rich cancer cells by NMR and molecular modeling.
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Bioorg Med Chem. 2016 Jan 14;
Authors: Vasile F, Menchi G, Lenci E, Guarna A, Potenza D, Trabocchi A
Abstract
The binding features of a novel class of 'click chemistry'-derived RGD mimics with integrin ligand capability were studied toward ?v?3 integrin using STD-NMR...
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01-29-2016 04:20 PM
[NMR paper] NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines.
NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines.
Related Articles NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines.
Adv Exp Med Biol. 2015;870:49-122
Authors: Brutscher B, Felli IC, Gil-Caballero S, Hošek T, Kümmerle R, Piai A, Pierattelli R, Sólyom Z
Abstract
Thanks to recent improvements in NMR instrumentation, pulse sequence design, and...
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09-21-2015 03:01 PM
[NMR paper] Insight into the modulation of Shaw2 Kv channels by general anesthetics: structural and functional studies of S4-S5 linker and S6 C-terminal peptides in micelles by NMR.
Insight into the modulation of Shaw2 Kv channels by general anesthetics: structural and functional studies of S4-S5 linker and S6 C-terminal peptides in micelles by NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Insight into the modulation of Shaw2 Kv channels by general anesthetics: structural and functional studies of S4-S5 linker and S6 C-terminal peptides in micelles by NMR.
Biochim Biophys Acta. 2013 Feb;1828(2):595-601
Authors: Zhang J, Qu X, Covarrubias M,...
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04-05-2013 10:53 AM
[NMR paper] General framework for studying the dynamics of folded and nonfolded proteins by NMR r
General framework for studying the dynamics of folded and nonfolded proteins by NMR relaxation spectroscopy and MD simulation.
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J Am Chem Soc. 2002 Apr 24;124(16):4522-34
Authors: Prompers JJ, Brüschweiler R
A general framework is presented for the interpretation of NMR relaxation data of proteins. The method, termed isotropic reorientational eigenmode dynamics (iRED), relies on a principal component...
[NMR paper] A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TO
A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments.
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J Biomol NMR. 1993 Mar;3(2):225-31
Authors: Logan TM, Olejniczak ET, Xu RX, Fesik SW
A general approach for assigning the resonances of uniformly 15N- and 13C-labeled proteins in their unfolded state is presented. The assignment approach takes advantage of the spectral dispersion of the amide...
A General Approach Towards Triazole-linked Adenosine Diphosphate Ribosylated Peptides and Proteins
Linear Mode
