[NMR paper] Protein Yoga: Conformational Versatility of the Hemolysin II C-terminal Domain Detailed by NMR Structures for Multiple States
Protein Yoga: Conformational Versatility of the Hemolysin II C-terminal Domain Detailed by NMR Structures for Multiple States
The C-terminal domain of Bacillus cereus hemolysin II, HlyIIC, stabilizes the trans-membrane-pore formed by the HlyII toxin and may aid in target cell recognition. Initial efforts to determine the NMR structure of HlyIIC were hampered by cis/trans isomerization about the single proline at position 405, that leads to doubling of NMR resonances. We used the mutant P405M-HlyIIC that eliminates the cis proline to determine the NMR structure of the domain, which revealed...
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03-20-2021 02:31 AM
Protein Yoga: Conformational Versatility of the Hemolysin II C-terminal Domain Detailed by NMR Structures for Multiple States
Protein Yoga: Conformational Versatility of the Hemolysin II C-terminal Domain Detailed by NMR Structures for Multiple States
ABSTRACT
The C-terminal domain of Bacillus cereus hemolysin II, HlyIIC, stabilizes the trans-membrane-pore formed by the HlyII toxin and may aid in target cell recognition. Initial efforts to determine the NMR structure of HlyIIC were hampered by cis/trans isomerization about the single proline at position 405, that leads to doubling of NMR resonances. We used the mutant P405M-HlyIIC that eliminates the cis proline to determine the NMR structure of the domain,...
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03-18-2021 05:17 PM
[ASAP] Protein–Ligand Interactions in the STING Binding Site Probed by Rationally Designed Single-Point Mutations: Experiment and Theory
Protein–Ligand Interactions in the STING Binding Site Probed by Rationally Designed Single-Point Mutations: Experiment and Theory
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00949/20210215/images/medium/bi0c00949_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00949
http://feeds.feedburner.com/~r/acs/bichaw/~4/JqMF5MXiewc
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02-18-2021 03:17 PM
[NMR paper] Bioorthogonal Catalytic Activation Of Pt And Ru Anticancer Complexes By FAD And Flavoproteins
Bioorthogonal Catalytic Activation Of Pt And Ru Anticancer Complexes By FAD And Flavoproteins
Recent advances in bioorthogonal catalysis promise to deliver new chemical tools for performing chemoselective transformations in complex biological environments. Herein we report how FAD (flavin adenine dinucleotide), FMN (flavin mononucleotide) and four flavoproteins behave as unconventional photocatalysts capable of converting PtIV and RuII complexes into potentially toxic PtII or RuII-OH2 species. Using electron donors and low doses of visible light, the flavoproteins mini Singlet Oxygen...
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01-23-2018 03:50 PM
[NMR paper] NMR study of mutations of glycine-52 of the catalytic domain of diphtheria toxin.
NMR study of mutations of glycine-52 of the catalytic domain of diphtheria toxin.
NMR study of mutations of glycine-52 of the catalytic domain of diphtheria toxin.
J Pharm Biomed Anal. 2017 Dec 02;150:72-79
Authors: Sauvé S, Gingras G, Aubin Y
Abstract
Cross-reacting-material 197 (CRM197) is a naturally occurring non-toxic mutant of diphtheria toxin (DT) that is one of the few carrier protein used in the manufacture of polysaccharide vaccines targeting bacterial pathogens such as Neisseria meningitidis, Streptococcus...
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12-08-2017 02:25 PM
Study shows how mutations disrupt ALS-linked protein - Science Codex
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Study shows how mutations disrupt ALS-linked protein
Science Codex
Using nuclear magnetic resonance, computer simulations and microscopy, Fawzi, Brown graduate student Alexander Conicella and colleagues at Lehigh University were able to show that under normal circumstances, TDP-43 molecules concentrate into little ...
Study shows how mutations disrupt ALS-linked protein - Science Codex
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08-19-2016 05:49 PM
Persistent Activation of cGMP-Dependent Protein Kinaseby a Nitrated Cyclic Nucleotide via Site Specific Protein S-Guanylation
Persistent Activation of cGMP-Dependent Protein Kinaseby a Nitrated Cyclic Nucleotide via Site Specific Protein S-Guanylation
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b00774/20160129/images/medium/bi-2015-00774n_0003.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b00774
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/KLjU9u3Nnwk
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