[NMR paper] Selective 1Halpha NMR methods to reveal functionally relevant proline cis/trans isomers in IDPs: characterization of minor forms, effects of phosphorylation and occurrence in proteome
Selective 1Halpha NMR methods to reveal functionally relevant proline cis/trans isomers in IDPs: characterization of minor forms, effects of phosphorylation and occurrence in proteome
Identification of proline cis/trans isomers appearing in several regulatory mechanisms of proteins and characterization of minor species present due to the conformational heterogeneity in IDPs is highly important. To obtain residue level information on these mobile systems we introduce two 1 H ? -detected, proline selective, real-time homodecoupled NMR experiments and analyze the proline abundant transactivation domain of p53. The measurements are sensitive enough to identify minor conformers...
[NMR paper] Multiple Site-Specific Phosphorylation of IDPs Monitored by NMR.
Multiple Site-Specific Phosphorylation of IDPs Monitored by NMR.
Related Articles Multiple Site-Specific Phosphorylation of IDPs Monitored by NMR.
Methods Mol Biol. 2020;2141:793-817
Authors: Julien M, Bouguechtouli C, Alik A, Ghouil R, Zinn-Justin S, Theillet FX
Abstract
In line with their high accessibility, disordered proteins are exquisite targets of kinases. Eukaryotic organisms use the so-called intrinsically disordered proteins (IDPs) or intrinsically disordered regions of proteins (IDRs) as molecular switches...
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[NMR paper] Altered Domain Structure of the Prion Protein Caused by Cu2+ Binding and Functionally Relevant Mutations: Analysis by Cross-Linking, MS/MS, and NMR.
Altered Domain Structure of the Prion Protein Caused by Cu2+ Binding and Functionally Relevant Mutations: Analysis by Cross-Linking, MS/MS, and NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Altered Domain Structure of the Prion Protein Caused by Cu2+ Binding and Functionally Relevant Mutations: Analysis by Cross-Linking, MS/MS, and NMR.
Structure. 2019 Mar 28;:
Authors: McDonald AJ, Leon DR, Markham KA, Wu B, Heckendorf CF, Schilling K, Showalter HD,...
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[ASAP] Coupling Green Fluorescent Protein Expression with Chemical Modification to Probe Functionally Relevant Riboswitch Conformations in Live Bacteria
Coupling Green Fluorescent Protein Expression with Chemical Modification to Probe Functionally Relevant Riboswitch Conformations in Live Bacteria
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00316/20180626/images/medium/bi-2018-003163_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00316
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[NMR paper] NMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif.
NMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles NMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif.
Structure. 2017 Mar 07;25(3):446-457
Authors: Chadwick AC, Jensen DR, Hanson PJ, Lange PT, Proudfoot SC, Peterson FC, Volkman BF, Sahoo D
...
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Tryptophan-Rich Sensory Protein/Translocator Protein(TSPO) from Cyanobacterium Fremyella diplosiphon Bindsa Broad Range of Functionally Relevant Tetrapyrroles
Tryptophan-Rich Sensory Protein/Translocator Protein(TSPO) from Cyanobacterium Fremyella diplosiphon Bindsa Broad Range of Functionally Relevant Tetrapyrroles
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b01019/20161216/images/medium/bi-2016-01019r_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b01019
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12-19-2016 07:58 PM
[NMR paper] NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain.
NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain.
Related Articles NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain.
Biomol NMR Assign. 2013 Nov 15;
Authors: Kaplan AR, Maciejewski MW, Olson R, Alexandrescu AT
Abstract
Pathogenic bacteria secrete pore-forming toxins (PFTs) to selectively defend against immune cells and to break through cellular barriers in the host. Understanding how PFTs attack cell membranes is not only essential for therapeutic intervention but for...
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[NMR paper] Multiple cis-trans conformers of the prolactin receptor proline-rich motif (PRM) pept
Multiple cis-trans conformers of the prolactin receptor proline-rich motif (PRM) peptide detected by reverse-phase HPLC, CD and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.biochemj.org-images-bj_pubmed.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Multiple cis-trans conformers of the prolactin receptor proline-rich motif (PRM) peptide detected by reverse-phase HPLC, CD and NMR spectroscopy.
Biochem J. 1996 May 1;315 ( Pt 3):833-44
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[NMR paper] The rate and structural consequences of proline cis-trans isomerization in calbindin
The rate and structural consequences of proline cis-trans isomerization in calbindin D9k: NMR studies of the minor (cis-Pro43) isoform and the Pro43Gly mutant.
Related Articles The rate and structural consequences of proline cis-trans isomerization in calbindin D9k: NMR studies of the minor (cis-Pro43) isoform and the Pro43Gly mutant.
Biochemistry. 1990 May 8;29(18):4400-9
Authors: Kördel J, Forsén S, Drakenberg T, Chazin WJ
The EF-hand calcium-binding protein, calbindin D9k, exists in solution in the calcium-loaded state, as a 1:3...
Selective 1Halpha NMR methods to reveal functionally relevant proline cis/trans isomers in IDPs: characterization of minor forms, effects of phosphorylation and occurrence in proteome
Linear Mode
