[NMR paper] Coupling Aptamer-based Protein Tagging with Metabolic Glycan Labeling for In Situ Visualization and Biological Function Study of Exosomal Protein-Specific Glycosylation
Coupling Aptamer-based Protein Tagging with Metabolic Glycan Labeling for In Situ Visualization and Biological Function Study of Exosomal Protein-Specific Glycosylation
[NMR paper] Automated glycan assembly of 19F labelled glycan probes enables high-throughput NMR studies of protein-glycan interactions
Automated glycan assembly of 19F labelled glycan probes enables high-throughput NMR studies of protein-glycan interactions
Protein-glycan interactions mediate important biological processes, including pathogen host invasion and cellular communication. Major challenges to monitoring these low affinity interactions are the required high sensitivity of a biophysical assay and to cover a breath of synthetic well-defined structures. Here, we showcase an expedite approach that integrates automated glycan assembly (AGA) of 19 F labelled probes and high-throughput NMR methods, enabling the study...
Using Chemical Synthesis To Study and Apply Protein Glycosylation
Using Chemical Synthesis To Study and Apply Protein Glycosylation
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b01055/20180114/images/medium/bi-2017-010556_0015.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b01055
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/KmLgiLrr4Rc
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01-17-2018 05:28 AM
Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register #DNPNMR
From The DNP-NMR Blog:
Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register #DNPNMR
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Frederick, K.K., et al., Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register. Proc. Nat. Aca. Sci. USA, 2017. 114(14): p. 3642-3647.
http://www.pnas.org/content/114/14/3642.abstract
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04-24-2017 02:56 PM
Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register [Biophysics and Computational Biology]
Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register
Kendra K. Frederick, Vladimir K. Michaelis, Marc A. Caporini, Loren B. Andreas, Galia T. Debelouchina, Robert G. Griffin, Susan Lindquist...
Date: 2017-04-04
The yeast prion protein Sup35NM is a self-propagating amyloid. Despite intense study, there is no consensus on the organization of monomers within Sup35NM fibrils. Some studies point to a ?-helical arrangement, whereas others suggest a parallel in-register organization. Intermolecular contacts are often...
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04-04-2017 10:41 PM
[NMR paper] Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register.
Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register.
Related Articles Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register.
Proc Natl Acad Sci U S A. 2017 Mar 22;:
Authors: Frederick KK, Michaelis VK, Caporini MA, Andreas LB, Debelouchina GT, Griffin RG, Lindquist S
Abstract
The yeast prion protein Sup35NM is a self-propagating amyloid. Despite intense study, there is no consensus on...
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03-24-2017 10:14 PM
Protein resonance assignment at MAS frequencies approaching 100Â*kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods
Protein resonance assignment at MAS frequencies approaching 100Â*kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods
Abstract
We discuss the optimum experimental conditions to obtain assignment spectra for solid proteins at magic-angle spinning (MAS) frequencies around 100Â*kHz. We present a systematic examination of the MAS dependence of the amide proton T 2â?² times and a site-specific comparison of T 2â?² at 93Â*kHz versus 60Â*kHz MAS frequency. A...
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08-13-2015 02:00 PM
[NMR paper] Labeling of recombinant protein for NMR spectroscopy: global and specific labeling of
Labeling of recombinant protein for NMR spectroscopy: global and specific labeling of the rat liver fructose 2,6-bisphosphatase domain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Labeling of recombinant protein for NMR spectroscopy: global and specific labeling of the rat liver fructose 2,6-bisphosphatase domain.
Protein Expr Purif. 1997 Oct;11(1):79-85
Authors: Okar DA, Felicia ND, Gui L, Lange AJ
Methods for the efficient use of the 13C-labeled nutrients,...