Dusquetide is a next-generation IDR (innate defense regulator) targeting the major autophagy receptor protein SQSTM1/p62 and modulating the innate immune response. Here, we describe a protocol for determining dusquetide-binding sites of p62 by solution NMR spectroscopy. Step-by-step technique details were provided, including sample preparation, NMR experiment setup, data processing, and binding site analysis. This protocol could be applied to characterize other small molecules targeting the ZZ...
[NMR paper] The effect of drug binding on specific sites in transmembrane helices 4 and 6 of the ABC exporter MsbA studied by DNP-enhanced solid-state NMR.
The effect of drug binding on specific sites in transmembrane helices 4 and 6 of the ABC exporter MsbA studied by DNP-enhanced solid-state NMR.
Related Articles The effect of drug binding on specific sites in transmembrane helices 4 and 6 of the ABC exporter MsbA studied by DNP-enhanced solid-state NMR.
Biochim Biophys Acta. 2017 Oct 22;:
Authors: Spadaccini R, Kaur H, Becker-Baldus J, Glaubitz C
Abstract
MsbA, a homodimeric ABC exporter, translocates its native substrate lipid A as well as a range of smaller, amphiphilic...
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10-28-2017 08:03 AM
[NMR paper] Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A.
Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A.
Related Articles Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A.
Biophys J. 2017 May 09;112(9):1820-1828
Authors: Kawamura T, Wakamoto T, Kitazawa S, Sakuraba S, Kameda T, Kitahara R
Abstract
Internal cavities in proteins produce conformational fluctuations and enable the binding of small ligands. Here, we report a NMR analysis of O2-binding sites by O2-induced paramagnetic...
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05-13-2017 02:08 PM
Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A
Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A
Publication date: 9 May 2017
Source:Biophysical Journal, Volume 112, Issue 9</br>
Author(s): Takahiro Kawamura, Takuro Wakamoto, Soichiro Kitazawa, Shun Sakuraba, Tomoshi Kameda, Ryo Kitahara</br>
Internal cavities in proteins produce conformational fluctuations and enable the binding of small ligands. Here, we report a NMR analysis of O2-binding sites by O2-induced paramagnetic relaxation enhancements (PREs) on amide groups of proteins in solution. Outer...
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05-10-2017 06:52 AM
[NMR paper] Using (15) N-Ammonium to Characterise and Map Potassium Binding Sites in Proteins by NMR Spectroscopy.
Using (15) N-Ammonium to Characterise and Map Potassium Binding Sites in Proteins by NMR Spectroscopy.
Related Articles Using (15) N-Ammonium to Characterise and Map Potassium Binding Sites in Proteins by NMR Spectroscopy.
Chembiochem. 2014 Feb 12;
Authors: Werbeck ND, Kirkpatrick J, Reinstein J, Hansen DF
Abstract
A variety of enzymes are activated by the binding of potassium ions. The potassium binding sites of these enzymes are very specific, but ammonium ions can often replace potassium ions in vitro because of their similar ionic...
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02-13-2014 03:35 PM
Small-Molecule Binding Sites on Proteins Establishedby Paramagnetic NMR Spectroscopy
Small-Molecule Binding Sites on Proteins Establishedby Paramagnetic NMR Spectroscopy
Jia-Ying Guan, Peter H. J. Keizers, Wei-Min Liu, Frank Lo?hr, Simon P. Skinner, Edwin A. Heeneman, Harald Schwalbe, Marcellus Ubbink and Gregg Siegal
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja401323m/aop/images/medium/ja-2013-01323m_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja401323m
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/ZukfjIRmQq8
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04-05-2013 11:03 PM
[NMR paper] Small molecule binding sites on proteins established by paramagnetic NMR spectroscopy.
Small molecule binding sites on proteins established by paramagnetic NMR spectroscopy.
Related Articles Small molecule binding sites on proteins established by paramagnetic NMR spectroscopy.
J Am Chem Soc. 2013 Mar 20;
Authors: Guan JY, Keizers PH, Liu WM, Loehr F, Skinner SP, Heeneman EA, Schwalbe H, Ubbink M, Siegal GD
Abstract
Determining the three dimensional structure of a small molecule-protein complex with weak affinity can be a significant challenge. We present a paramagnetic NMR method to determine intermolecular structure...
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03-21-2013 02:58 PM
Engineering [Ln(DPA)3]3â?? binding sites in proteins: a widely applicable method for tagging proteins with lanthanide ions
Engineering 3â?? binding sites in proteins: a widely applicable method for tagging proteins with lanthanide ions
Abstract Paramagnetic relaxation enhancements from unpaired electrons observed in nuclear magnetic resonance (NMR) spectra present powerful long-range distance restraints. The most frequently used paramagnetic tags, however, are tethered to the protein via disulfide bonds, requiring proteins with single cysteine residues for covalent attachment. Here we present a straightforward strategy to tag proteins site-specifically with paramagnetic lanthanides without a tether and...
Protocol to identify drug-binding sites in proteins using solution NMR spectroscopy
Linear Mode
