[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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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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[NMR paper] Applications of NMR-based PRE and EPR-based DEER spectroscopy to homodimer chain exchange characterization and structure determination.
Applications of NMR-based PRE and EPR-based DEER spectroscopy to homodimer chain exchange characterization and structure determination.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Applications of NMR-based PRE and EPR-based DEER spectroscopy to homodimer chain exchange characterization and structure determination.
Methods Mol Biol. 2014;1091:215-27
Authors: Yang Y, Ramelot TA, Ni S, McCarrick RM, Kennedy MA
Abstract
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Unusual Structural Features Revealed by the SolutionNMR Structure of the NLRC5 Caspase Recruitment Domain
Unusual Structural Features Revealed by the SolutionNMR Structure of the NLRC5 Caspase Recruitment Domain
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi500177x/aop/images/medium/bi-2014-00177x_0007.gif
Biochemistry
DOI: 10.1021/bi500177x
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[NMR paper] The H/D-exchange Kinetics of the Escherichia coli Co-chaperonin GroES Studied by 2D-NMR and DMSO-Quenched Exchange Methods.
The H/D-exchange Kinetics of the Escherichia coli Co-chaperonin GroES Studied by 2D-NMR and DMSO-Quenched Exchange Methods.
Related Articles The H/D-exchange Kinetics of the Escherichia coli Co-chaperonin GroES Studied by 2D-NMR and DMSO-Quenched Exchange Methods.
J Mol Biol. 2013 Apr 11;
Authors: Chandak MS, Nakamura T, Makabe K, Takenaka T, Mukaiyama A, Chaudhuri TK, Kato K, Kuwajima K
Abstract
We studied hydrogen/deuterium-exchange reactions of peptide amide protons of GroES using two different techniques: (1) two-dimensional (1)H-(15)N...
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04-16-2013 07:46 PM
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy
Abstract We developed a new method to elucidate the binding kinetics kon and koff, and the dissociation constant KD (=koff/kon), of protein-protein interactions without observable bound resonances of the protein of interest due to high molecular weight in a complex with a large target protein. In our method, kon and koff rates are calculated from the analysis of longitudinal relaxation rates of free resonances measured for multiple samples containing different...
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[NMR paper] Hydrogen exchange kinetics in a membrane protein determined by 15N NMR spectroscopy:
Hydrogen exchange kinetics in a membrane protein determined by 15N NMR spectroscopy: use of the INEPT experiment to follow individual amides in detergent-solubilized M13 coat protein.
Related Articles Hydrogen exchange kinetics in a membrane protein determined by 15N NMR spectroscopy: use of the INEPT experiment to follow individual amides in detergent-solubilized M13 coat protein.
Biochemistry. 1990 Jul 3;29(26):6303-13
Authors: Henry GD, Sykes BD
The coat protein of the filamentous coliphage M13 is a 50-residue polypeptide which spans the...
GlobalDynamics and Exchange Kinetics of a Proteinon the Surface of Nanoparticles Revealed by Relaxation-Based SolutionNMR Spectroscopy
Linear Mode
