Solid-state nuclear magnetic resonance (NMR) methods can probe the motions of membrane proteins in liposomes at the atomic level, and propel the understanding of biomolecular processes for which static structures cannot provide a satisfactory description. High-resolution crystallography snapshots have provided a structural basis for fluoride channels. NMR is a powerful tool to build upon these snapshots and depict a dynamic picture of fluoride channels in native-like lipid bilayers. In this...
[NMR paper] Saturation transfer difference NMR on the integral trimeric membrane transport protein GltPh determines cooperative substrate binding.
Saturation transfer difference NMR on the integral trimeric membrane transport protein GltPh determines cooperative substrate binding.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.nature.com-images-npg_logo.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.png Saturation transfer difference NMR on the integral trimeric membrane transport protein GltPh determines...
[NMR paper] Solid-state NMR methods for oriented membrane proteins.
Solid-state NMR methods for oriented membrane proteins.
Related Articles Solid-state NMR methods for oriented membrane proteins.
Prog Nucl Magn Reson Spectrosc. 2015 Aug;88-89:48-85
Authors: Hansen SK, Bertelsen K, Paaske B, Nielsen NC, Vosegaard T
Abstract
Oriented-sample solid-state NMR represents one of few experimental methods capable of characterising the membrane-bound conformation of proteins in the cell membrane. Since the technique was developed 25 years ago, the technique has been applied to study the structure of helix...
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08-19-2015 03:24 PM
Solid-State NMR Methods for Oriented Membrane Proteins
Solid-State NMR Methods for Oriented Membrane Proteins
Publication date: Available online 19 May 2015
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Sara K. Hansen , Kresten Bertelsen , Berit Paaske , Niels Chr. Nielsen , Thomas Vosegaard</br>
Oriented-sample solid-state NMR represents one of few experimental methods capable of characterising the membrane-bound conformation of proteins in the cell membrane. Since the technique was developed 25 years ago, the technique has been applied to study the structure of helix bundle membrane...
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05-19-2015 09:10 AM
[NMR paper] Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods.
Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods.
Related Articles Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods.
Anal Biochem. 2013 Dec 9;
Authors: Sahu D, Bastidas M, Showalter S
Abstract
There is an extraordinary need to describe the structures of intrinsically disordered proteins (IDPs) due to their role in various biological processes involved in signaling and transcription. However, general study of IDPs...
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12-18-2013 04:00 PM
Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods
Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods
Publication date: Available online 10 December 2013
Source:Analytical Biochemistry</br>
Author(s): Debashish Sahu , Monique Bastidas , Scott Showalter</br>
There is an extraordinary need to describe the structures of intrinsically disordered proteins (IDPs) due to their role in various biological processes involved in signaling and transcription. However, general study of IDPs by NMR spectroscopy is limited by the poor 1H-amide chemical shift dispersion...
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12-10-2013 04:48 AM
Dynamic nuclear polarization methods in solids and solutions to explore membrane proteins and membrane systems
From The DNP-NMR Blog:
Dynamic nuclear polarization methods in solids and solutions to explore membrane proteins and membrane systems
Cheng, C.Y. and S. Han, Dynamic nuclear polarization methods in solids and solutions to explore membrane proteins and membrane systems. Annu Rev Phys Chem, 2013. 64(1): p. 507-32.
http://www.ncbi.nlm.nih.gov/pubmed/23331309
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07-08-2013 02:17 PM
[NMR paper] Weak substrate binding to transport proteins studied by NMR.
Weak substrate binding to transport proteins studied by NMR.
Related Articles Weak substrate binding to transport proteins studied by NMR.
Biophys J. 1998 Dec;75(6):2794-800
Authors: Spooner PJ, O'Reilly WJ, Homans SW, Rutherford NG, Henderson PJ, Watts A
The weak binding of sugar substrates fails to induce any quantifiable physical changes in the L-fucose-H+ symport protein, FucP, from Escherichia coli, and this protein lacks any strongly binding ligands for competitive binding assays. Access to substrate binding behavior is however possible...