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 line broadening, ?R2. By combined analysis of ?R2 profiles arising from interactions with liposomes of varying sizes, an approach recently developed for the characterization of interactions of mono-ubiquitin with liposomes, we determine how the parameters of exchange (liposome binding) and dynamics of each individual domain of Ub2 on the surface of liposomes change when the domains are covalently attached to one another by a flexible linker. Two different covalent linkages were used: K63-linked and K48-linked Ub2. The possibility of three distinct modes of binding of Ub2 to liposomes requires the introduction of simple but important modifications to the strategy of analysis originally developed for mono-ubiquitin.
PMID: 28530812 [PubMed - as supplied by publisher]
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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[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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NMR approaches in structure-based lead discovery: Recent developments and new frontiers for targeting multi-protein complexes
NMR approaches in structure-based lead discovery: Recent developments and new frontiers for targeting multi-protein complexes
Publication date: Available online 28 August 2014
Source:Progress in Biophysics and Molecular Biology</br>
Author(s): David M. Dias , Alessio Ciulli</br>
Nuclear magnetic resonance (NMR) spectroscopy is a pivotal method for structure-based and fragment-based lead discovery because it is one of the most robust techniques to provide information on protein structure, dynamics and interaction at an atomic level in solution. Nowadays, in most...
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[NMR paper] Comparing Binding Modes of Analogous Fragments Using NMR in Fragment-Based Drug Design: Application to PRDX5.
Comparing Binding Modes of Analogous Fragments Using NMR in Fragment-Based Drug Design: Application to PRDX5.
Comparing Binding Modes of Analogous Fragments Using NMR in Fragment-Based Drug Design: Application to PRDX5.
PLoS One. 2014;9(7):e102300
Authors: Aguirre C, Brink TT, Guichou JF, Cala O, Krimm I
Abstract
Fragment-based drug design is one of the most promising approaches for discovering novel and potent inhibitors against therapeutic targets. The first step of the process consists of identifying fragments that bind...
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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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[NMR paper] Probing the cation binding modes of macrocyclic HCV protease inhibitor BILN 2061 by multinuclear NMR.
Probing the cation binding modes of macrocyclic HCV protease inhibitor BILN 2061 by multinuclear NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Probing the cation binding modes of macrocyclic HCV protease inhibitor BILN 2061 by multinuclear NMR.
J Pharm Biomed Anal. 2012 Nov;70:609-13
Authors: Busacca CA, Jones PJ, Campbell SJ, Saha AK, Gonnella NC, Senanayake CH
Abstract
The ability of the macrocyclic HCV protease inhibitor BILN 2061 to bind different...
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[NMR paper] Interpretation of NMR relaxation properties of Pin1, a two-domain protein, based on B
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J Biomol NMR. 2004 May;29(1):21-35
Authors: Bernadó P, Fernandes MX, Jacobs DM, Fiebig K, García de la Torre J, Pons M
Many important proteins contain multiple domains connected by flexible linkers. Inter-domain motion is suggested to play a key role in many processes involving molecular recognition....
Probing the Binding Modes of a Multi-Domain Protein to Lipid-Based Nanoparticles by Relaxation-Based NMR.
Linear Mode
