[NMR paper] Carbene footprinting reveals binding interfaces of a multimeric membrane spanning protein
Carbene footprinting reveals binding interfaces of a multimeric membrane spanning protein
Mapping the interaction sites between membrane spanning proteins is a key challenge in structural biology. In this study a carbene footprinting approach is developed and applied to identify the interfacial sites of a trimeric, integral membrane protein, OmpF, solubilised in micelles. The diazirine-based footprinting probe is effectively sequestered by, and incorporated into, the micelles leading to efficient labelling of the membrane-spanning regions of the protein upon irradiation at 349 nm. Areas...
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09-27-2017 04:26 PM
Dynamic Nuclear Polarization/Solid-State NMR Spectroscopy of Membrane Polypeptides: Free-Radical Optimization for Matrix-Free Lipid Bilayer Samples #DNPNMR
From The DNP-NMR Blog:
Dynamic Nuclear Polarization/Solid-State NMR Spectroscopy of Membrane Polypeptides: Free-Radical Optimization for Matrix-Free Lipid Bilayer Samples #DNPNMR
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Salnikov, E.S., et al., Dynamic Nuclear Polarization/Solid-State NMR Spectroscopy of Membrane Polypeptides: Free-Radical Optimization for Matrix-Free Lipid Bilayer Samples. ChemPhysChem, 2017. 18(15): p. 2103-2113.
https://www.ncbi.nlm.nih.gov/pubmed/28574169
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09-25-2017 08:42 PM
[NMR paper] Laser-initiated Radical Trifluoromethylation of Peptides and Proteins and Its Application to Mass Spectrometry-Based Protein Footprinting
Laser-initiated Radical Trifluoromethylation of Peptides and Proteins and Its Application to Mass Spectrometry-Based Protein Footprinting
We describe a novel, laser-initiated radical trifluoromethylation for protein footprinting and establish its broad residue coverage. *CF3 reacts with 18 of 20 common amino acids including Gly, Ala, Ser, Thr, Asp, Glu that are relatively "silent" with *OH. This new approach to footprinting is a bridge between trifluoromethylation in materials and medicinal chemistry and structural biology and biotechnology. Its application to a membrane protein and to...
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09-13-2017 08:48 PM
[NMR paper] Dynamic nuclear polarization / solid-state NMR of membrane polypeptides. Free radical optimization for matrix-free lipid bilayer samples.
Dynamic nuclear polarization / solid-state NMR of membrane polypeptides. Free radical optimization for matrix-free lipid bilayer samples.
Related Articles Dynamic nuclear polarization / solid-state NMR of membrane polypeptides. Free radical optimization for matrix-free lipid bilayer samples.
Chemphyschem. 2017 Jun 02;:
Authors: Ouari O, Salnikov ES, Abel S, Karthikeyan G, Karoui H, Aussenac F, Tordo P, Bechinger B
Abstract
Dynamic Nuclear Polarization boosts the sensitivity of NMR spectroscopy by orders of magnitude making...
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06-03-2017 11:49 AM
Structural Analysis of the Glycosylated Intact HIV-1 gp120–b12 Antibody Complex Using Hydroxyl Radical Protein Footprinting
Structural Analysis of the Glycosylated Intact HIV-1 gp120–b12 Antibody Complex Using Hydroxyl Radical Protein Footprinting
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00888/20170206/images/medium/bi-2016-008884_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00888
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/yGaVonLnOfQ
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02-07-2017 04:14 AM
Detergent-free Isolation of Functional G Protein-CoupledReceptors into Nanometric Lipid Particles
Detergent-free Isolation of Functional G Protein-CoupledReceptors into Nanometric Lipid Particles
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01040/20151223/images/medium/bi-2015-01040n_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01040
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/Mw6e22AdGJI
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12-28-2015 12:26 AM
[NMR paper] NMR study of a membrane protein in detergent-free aqueous solution.
NMR study of a membrane protein in detergent-free aqueous solution.
Related Articles NMR study of a membrane protein in detergent-free aqueous solution.
Proc Natl Acad Sci U S A. 2005 Jun 21;102(25):8893-8
Authors: Zoonens M, Catoire LJ, Giusti F, Popot JL
One of the major obstacles to membrane protein (MP) structural studies is the destabilizing effect of detergents. Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep MPs water-soluble under mild conditions. In the present work, we have explored the...
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11-25-2010 08:21 PM
[NMR paper] NMR structures of the C-terminal segment of surfactant protein B in detergent micelle
NMR structures of the C-terminal segment of surfactant protein B in detergent micelles and hexafluoro-2-propanol.
Related Articles NMR structures of the C-terminal segment of surfactant protein B in detergent micelles and hexafluoro-2-propanol.
Biochemistry. 2004 Dec 7;43(48):15187-94
Authors: Booth V, Waring AJ, Walther FJ, Keough KM
Although the membrane-associated surfactant protein B (SP-B) is an essential component of lung surfactant, which is itself essential for life, the molecular basis for its activity is not understood. SP-B's...