We probed the "dark" state involved in the protein-quantum dot (QD) interaction using a relaxation-based solution nuclear magnetic resonance (NMR) approach. We examined the dynamics and exchange kinetics of the ubiquitin-CdTe model system, which undergoes a fast exchange in the transverse relaxation time scale. We applied the recently developed dark-state exchange saturation transfer (DEST), lifetime line broadening (?R(2)), and exchange-induced chemical shift (?(ex)) solution NMR techniques to...
[NMR paper] Dynamics of Bacteriorhodopsin in the Dark-Adapted State from Solution NMR.
Dynamics of Bacteriorhodopsin in the Dark-Adapted State from Solution NMR.
Dynamics of Bacteriorhodopsin in the Dark-Adapted State from Solution NMR.
Angew Chem Int Ed Engl. 2020 Jul 29;:
Authors: Kooijman L, Schuster M, Baumann C, Jurt S, Löhr F, Fürtig B, Güntert P, Zerbe O
Abstract
To achieve efficient proton pumping in the light-driven proton pump bacteriorhodopsin, the protein must be tightly coupled to the retinal to rapidly convert retinal isomerization into protein structural rearrangements. Methyl group dynamics of...
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[NMR paper] Probing the Atomic Structure of Transient Protein Contacts by Paramagnetic Relaxation Enhancement Solution NMR.
Probing the Atomic Structure of Transient Protein Contacts by Paramagnetic Relaxation Enhancement Solution NMR.
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Methods Mol Biol. 2018;1688:243-255
Authors: Venditti V, Fawzi NL
Abstract
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[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
[NMR paper] Visualizing transient dark states by NMR spectroscopy.
Visualizing transient dark states by NMR spectroscopy.
Visualizing transient dark states by NMR spectroscopy.
Q Rev Biophys. 2015 Feb;48(1):35-116
Authors: Anthis NJ, Clore GM
Abstract
Myriad biological processes proceed through states that defy characterization by conventional atomic-resolution structural biological methods. The invisibility of these 'dark' states can arise from their transient nature, low equilibrium population, large molecular weight, and/or heterogeneity. Although they are invisible, these dark states...
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[NMR paper] Frontispiece: probing transient conformational States of proteins by solid-state r1? relaxation-dispersion NMR spectroscopy.
Frontispiece: probing transient conformational States of proteins by solid-state r1? relaxation-dispersion NMR spectroscopy.
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Angew Chem Int Ed Engl. 2014 Apr 22;53(17)
Authors: Ma P, Haller JD, Zajakala J, Macek P, Sivertsen AC, Willbold D, Boisbouvier J,...
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[NMR paper] Probing Transient Conformational States of Proteins by Solid-State R1? Relaxation-Dispersion NMR Spectroscopy.
Probing Transient Conformational States of Proteins by Solid-State R1? Relaxation-Dispersion NMR Spectroscopy.
Related Articles Probing Transient Conformational States of Proteins by Solid-State R1? Relaxation-Dispersion NMR Spectroscopy.
Angew Chem Int Ed Engl. 2014 Mar 18;
Authors: Ma P, Haller JD, Zajakala J, Macek P, Sivertsen AC, Willbold D, Boisbouvier J, Schanda P
Abstract
The function of proteins depends on their ability to sample a variety of states differing in structure and free energy. Deciphering how the various thermally...
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[NMR paper] Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.
Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.
Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.
Proc Natl Acad Sci U S A. 2013 Jun 24;
Authors: Libich DS, Fawzi NL, Ying J, Clore GM
Abstract
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The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation
The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation
Available online 13 December 2012
Publication year: 2012
Source:Current Opinion in Structural Biology</br>
</br>
Historically it has been virtually impossible to experimentally determine the contribution of residual protein entropy to fundamental protein activities such as the binding of ligands. Recent progress has illuminated the possibility of employing NMR relaxation methods to quantitatively determine the role of changes in conformational...
Examining the Transient Dark State in Protein-Quantum Dot Interaction by Relaxation-Based Solution NMR
Linear Mode
