Peripheral membrane proteins can adopt distinct orientations on the surfaces of lipid bilayers that are often short-lived and challenging to characterize by conventional experimental methods. Here we describe a robust approach for mapping protein orientational landscapes through quantitative interpretation of paramagnetic relaxation enhancement (PRE) data arising from membrane mimetics with spin-labeled lipids. Theoretical analysis, followed by experimental verification, reveals insights into...
[NMR paper] Cu(II)-Based Paramagnetic Probe to Study RNA-Protein Interactions by NMR.
Cu(II)-Based Paramagnetic Probe to Study RNA-Protein Interactions by NMR.
Related Articles Cu(II)-Based Paramagnetic Probe to Study RNA-Protein Interactions by NMR.
Inorg Chem. 2017 Mar 22;
Authors: Seebald LM, DeMott CM, Ranganathan S, Asare Okai PN, Glazunova A, Chen A, Shekhtman A, Royzen M
Abstract
Paramagnetic NMR techniques allow for studying three-dimensional structures of RNA-protein complexes. In particular, paramagnetic relaxation enhancement (PRE) data can provide valuable information about long-range distances between...
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03-23-2017 08:51 PM
[NMR paper] Cobalt-based paramagnetic probe to study RNA-protein interactions by NMR.
Cobalt-based paramagnetic probe to study RNA-protein interactions by NMR.
Related Articles Cobalt-based paramagnetic probe to study RNA-protein interactions by NMR.
J Inorg Biochem. 2017 Feb 24;170:202-208
Authors: Seebald LM, DeMott CM, Ranganathan S, Asare-Okai PN, Glazunova A, Chen A, Shekhtman A, Royzen M
Abstract
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03-07-2017 08:54 PM
Cobalt-based paramagnetic probe to study RNA-protein interactions by NMR
Cobalt-based paramagnetic probe to study RNA-protein interactions by NMR
Publication date: Available online 24 February 2017
Source:Journal of Inorganic Biochemistry</br>
Author(s): Leah M. Seebald, Christopher M. DeMott, Srivathsan Ranganathan, Papa Nii Asare Okai, Anastasia Glazunova, Alan Chen, Alexander Shekhtman, Maksim Royzen</br>
Paramagnetic resonance enhancement (PRE) is an NMR technique that allows studying three-dimensional structures of RNA-protein complexes in solution. RNA strands are typically spin labeled using nitroxide reagents,...
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02-25-2017 06:21 AM
[NMR paper] Quantitative analysis of protein-ligand interactions by NMR.
Quantitative analysis of protein-ligand interactions by NMR.
Quantitative analysis of protein-ligand interactions by NMR.
Prog Nucl Magn Reson Spectrosc. 2016 Aug;96:47-57
Authors: Furukawa A, Konuma T, Yanaka S, Sugase K
Abstract
Protein-ligand interactions have been commonly studied through static structures of the protein-ligand complex. Recently, however, there has been increasing interest in investigating the dynamics of protein-ligand interactions both for fundamental understanding of the underlying mechanisms and for drug...
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08-31-2016 02:34 PM
Quantitative analysis of protein僕igand interactions by NMR
Quantitative analysis of protein僕igand interactions by NMR
Publication date: Available online 3 March 2016
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Ayako Furukawa, Tsuyoshi Konuma, Saeko Yanaka, Kenji Sugase</br>
Protein僕igand interactions have been commonly studied through static structures of the protein僕igand complex. Recently, however, there has been increasing interest in investigating the dynamics of protein僕igand interactions both for fundamental understanding of the underlying mechanisms and for drug development....
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03-03-2016 08:32 PM
[NMR paper] Solid-State NMR-Restrained Ensemble Dynamics of a Membrane Protein in Explicit Membranes.
Solid-State NMR-Restrained Ensemble Dynamics of a Membrane Protein in Explicit Membranes.
Related Articles Solid-State NMR-Restrained Ensemble Dynamics of a Membrane Protein in Explicit Membranes.
Biophys J. 2015 Apr 21;108(8):1954-1962
Authors: Cheng X, Jo S, Qi Y, Marassi FM, Im W
Abstract
Solid-state NMR has been used to determine the structures of membrane proteins in native-like lipid bilayer environments. Most structure calculations based on solid-state NMR observables are performed using simulated annealing with restrained...
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04-23-2015 06:11 PM
Solid-State NMR-Restrained Ensemble Dynamics of a Membrane Protein in Explicit Membranes
Solid-State NMR-Restrained Ensemble Dynamics of a Membrane Protein in Explicit Membranes
Publication date: 21 April 2015
Source:Biophysical Journal, Volume 108, Issue 8</br>
Author(s): Xi Cheng , Sunhwan Jo , Yifei Qi , Francesca*M. Marassi , Wonpil Im</br>
Solid-state NMR has been used to determine the structures of membrane proteins in native-like lipid bilayer environments. Most structure calculations based on solid-state NMR observables are performed using simulated annealing with restrained molecular dynamics and an energy function, where all nonbonded...
Quantitative Paramagnetic NMR-Based Analysis of Protein Orientational Dynamics on Membranes: Dissecting the KRas4B-Membrane Interactions
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