The global motions of ubiquitin, a model protein, on the surface of anisotropically tumbling 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1'-rac-glycerol) (POPG):1,2-dihexanoyl-sn-glycero-3-phosphocholine (DHPC) bicelles are described. The shapes of POPG:DHPC bicelles prepared with high molar ratios q of POPG to DHPC can be approximated by prolate ellipsoids, with the ratio of ellipsoid dimensions and dimensions themselves increasing with higher values of q. Adaptation of the nuclear magnetic...
[NMR paper] Dynamics of dehaloperoxidase-hemoglobin A derived from NMR relaxation spectroscopy and molecular dynamics simulation.
Dynamics of dehaloperoxidase-hemoglobin A derived from NMR relaxation spectroscopy and molecular dynamics simulation.
Dynamics of dehaloperoxidase-hemoglobin A derived from NMR relaxation spectroscopy and molecular dynamics simulation.
J Inorg Biochem. 2018 Jan 12;181:65-73
Authors: Zhao J, Xue M, Gudanis D, Gracz H, Findenegg GH, Gdaniec Z, Franzen S
Abstract
Dehaloperoxidase-hemoglobin is the first hemoglobin identified with biologically-relevant oxidative functions, which include peroxidase, peroxygenase and oxidase...
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02-07-2018 03:41 PM
[NMR paper] Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic T1? NMR Relaxation.
Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic T1? NMR Relaxation.
Related Articles Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic T1? NMR Relaxation.
Biophys J. 2018 Jan 23;114(2):392-399
Authors: Awosanya EO, Nevzorov AA
Abstract
A membrane-bound form of Pf1 coat protein reconstituted in magnetically aligned DMPC/DHPC bicelles was used as a molecular probe to quantify for the viscosity of the lipid membrane interior by measuring the uniaxial rotational diffusion...
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02-06-2018 07:42 PM
Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic T1? NMR Relaxation
Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic T1? NMR Relaxation
Publication date: 23 January 2018
Source:Biophysical Journal, Volume 114, Issue 2</br>
Author(s): Emmanuel O. Awosanya, Alexander A. Nevzorov</br>
A membrane-bound form of Pf1 coat protein reconstituted in magnetically aligned DMPC/DHPC bicelles was used as a molecular probe to quantify for the viscosity of the lipid membrane interior by measuring the uniaxial rotational diffusion coefficient of the protein. Orientationally dependent 15N NMR relaxation times in the...
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02-03-2018 02:16 PM
[NMR paper] Probing the Binding Modes of a Multi-Domain Protein to Lipid-Based Nanoparticles by Relaxation-Based NMR.
Probing the Binding Modes of a Multi-Domain Protein to Lipid-Based Nanoparticles by Relaxation-Based NMR.
Related Articles Probing the Binding Modes of a Multi-Domain Protein to Lipid-Based Nanoparticles by Relaxation-Based NMR.
J Phys Chem Lett. 2017 May 22;:
Authors: Ceccon A, Tugarinov V, Boughton AJ, Fushman D, Clore GM
Abstract
The interactions of two model multi-domain proteins - covalently linked di-ubiquitins, Ub2 - with lipid-based nanoparticles have been quantitatively probed by the measurements of NMR lifetime...
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05-23-2017 04:45 PM
GlobalDynamics and Exchange Kinetics of a Proteinon the Surface of Nanoparticles Revealed by Relaxation-Based SolutionNMR Spectroscopy
GlobalDynamics and Exchange Kinetics of a Proteinon the Surface of Nanoparticles Revealed by Relaxation-Based SolutionNMR Spectroscopy
Alberto Ceccon, Vitali Tugarinov, Ad Bax and G. Marius Clore
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b02654/20160427/images/medium/ja-2016-02654c_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b02654
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/edns7WqH1Ts
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04-28-2016 02:04 AM
[NMR paper] Global Dynamics and Exchange Kinetics of a Protein on the Surface of Nanoparticles Revealed by Relaxation-Based Solution NMR Spectroscopy.
Global Dynamics and Exchange Kinetics of a Protein on the Surface of Nanoparticles Revealed by Relaxation-Based Solution NMR Spectroscopy.
Global Dynamics and Exchange Kinetics of a Protein on the Surface of Nanoparticles Revealed by Relaxation-Based Solution NMR Spectroscopy.
J Am Chem Soc. 2016 Apr 25;
Authors: Ceccon A, Tugarinov V, Bax A, Clore GM
Abstract
The global motions and exchange kinetics of a model protein, ubiquitin, bound to the surface of negatively charged lipid-based nano-particles (liposomes) are derived from...
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04-26-2016 12:14 PM
Monitoring Protein Structure on the Surface of Gold Nanoparticles using NMR Spectroscopy
Monitoring Protein Structure on the Surface of Gold Nanoparticles using NMR Spectroscopy
Publication date: 27 January 2015
Source:Biophysical Journal, Volume 108, Issue 2, Supplement 1</br>
Author(s): Ailin Wang , Karen Woods , Tam Vo , Alex Coats , Nicholas C. Fitzkee</br>
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