Literature DB >> 27558624

Towards interpretation of intermolecular paramagnetic relaxation enhancement outside the fast exchange limit.

Alberto Ceccon1, G Marius Clore2, Vitali Tugarinov3.   

Abstract

In an exchanging system between major and minor species, the transverse paramagnetic relaxation enhancement rate observed on the resonances of the major species (Γ 2 (app) ) is dependent upon the exchange regime between the species. Quantitative analysis of PRE data in such systems typically assumes that the overall exchange rate k ex between the species is fast on the PRE time scale (k ex ≫ Γ2). Recently, we have characterized the kinetics of binding of the model protein ubiquitin to large (LUV) and small (SUV) unilamellar lipid-based nanoparticles or liposomes (Ceccon A, Tugarinov V, Bax A, Clore GM (2016). J Am Chem Soc 138:5789-5792). Building upon these results and taking advantage of a strong paramagnetic agent with an isotropic g-tensor, Gd(3+), we were able to measure intermolecular methyl carbon and proton PREs between paramagnetically-tagged liposomes and ubiquitin. In the limit of fast exchange (k ex ≫ Γ2) the ratio of the apparent proton to carbon methyl PREs, ((1)Hm-Γ 2 (app) )/((13)Cm-Γ 2 (app) ), is equal to the square of the ratio of the gyromagnetic ratios of the two nuclei, (γΗ/γC)(2). However, outside the fast exchange regime, under intermediate exchange conditions (e.g. when Γ2 is comparable in magnitude to k ex) the ((1)Hm-Γ 2 (app) )/((13)Cm-Γ 2 (app) ) ratio provides a reliable measure of the 'true' methyl PREs.

Entities:  

Keywords:  Chemical exchange; Ligand binding; Liposomes; Paramagnetic relaxation enhancement; Protein-nanoparticle interactions

Mesh:

Substances:

Year:  2016        PMID: 27558624     DOI: 10.1007/s10858-016-0053-x

Source DB:  PubMed          Journal:  J Biomol NMR        ISSN: 0925-2738            Impact factor:   2.835


  21 in total

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Journal:  J Phys Chem B       Date:  2007-02-01       Impact factor: 2.991

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Review 4.  Dynamics in electron transfer protein complexes.

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Review 5.  Solution NMR Structure Determination of Polytopic α-Helical Membrane Proteins: A Guide to Spin Label Paramagnetic Relaxation Enhancement Restraints.

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Journal:  Methods Enzymol       Date:  2015-03-17       Impact factor: 1.600

6.  Hsp70 biases the folding pathways of client proteins.

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7.  Persistent contrast enhancement by sterically stabilized paramagnetic liposomes in murine melanoma.

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8.  Global Dynamics and Exchange Kinetics of a Protein on the Surface of Nanoparticles Revealed by Relaxation-Based Solution NMR Spectroscopy.

Authors:  Alberto Ceccon; Vitali Tugarinov; Ad Bax; G Marius Clore
Journal:  J Am Chem Soc       Date:  2016-04-27       Impact factor: 15.419

Review 9.  Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.

Authors:  G Marius Clore; Junji Iwahara
Journal:  Chem Rev       Date:  2009-09       Impact factor: 60.622

10.  Echo-time and field strength dependence of BOLD reactivity in veins and parenchyma using flow-normalized hypercapnic manipulation.

Authors:  Christina Triantafyllou; Lawrence L Wald; Richard D Hoge
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  3 in total

1.  Probing the Binding Modes of a Multidomain Protein to Lipid-based Nanoparticles by Relaxation-based NMR.

Authors:  Alberto Ceccon; Vitali Tugarinov; Andrew J Boughton; David Fushman; G Marius Clore
Journal:  J Phys Chem Lett       Date:  2017-05-24       Impact factor: 6.475

2.  Exchange saturation transfer and associated NMR techniques for studies of protein interactions involving high-molecular-weight systems.

Authors:  Vitali Tugarinov; G Marius Clore
Journal:  J Biomol NMR       Date:  2019-08-12       Impact factor: 2.835

Review 3.  NMR methods for exploring 'dark' states in ligand binding and protein-protein interactions.

Authors:  Vitali Tugarinov; Alberto Ceccon; G Marius Clore
Journal:  Prog Nucl Magn Reson Spectrosc       Date:  2021-11-02       Impact factor: 9.795

  3 in total

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