Protein NMR on a chip: Development of an integrated microfluidic platform for studying protein-ligand interactions by nuclear magnetic resonance
Protein NMR on a chip: Development of an integrated microfluidic platform for studying protein-ligand interactions by nuclear magnetic resonance
This work demonstrates the performance of the integrated microfluidic sys tem for studying protein-ligand interactions by nuclear magnetic resonance (NMR). The platform couples together the advantages associated with microfluidic operation, i.e. minimised sample use and precision of operation, and characterisation by NMR. NMR offers unique capabilities for biomolecular research, relating to its non-invasive and non-destructive nature and atomic-scale resolution. This enables identification of the number and location of interaction sites, allosteric effects, atomic structures, dynamics of ligands and proteins, as well as full thermodynamic evaluation of the interaction. Integrating the aforementioned aspects can open new avenues for protein analysis, on one hand enhancing the usually limited throughput and functionality of NMR, on the other providing an extensive readout method to microfluidic systems, that can be fur ther linked with other analytical tools
Protein Binding, microfluidics, NMR, microfluidic-NMR
University of Southampton
Plata, Marek
4125895e-ff1c-48c9-835e-8e2c12c430b2
October 2023
Plata, Marek
4125895e-ff1c-48c9-835e-8e2c12c430b2
Utz, Marcel
c84ed64c-9e89-4051-af39-d401e423891b
Werner, J.M.
dd071d34-3db9-4141-9171-762b408b7539
Plata, Marek
(2023)
Protein NMR on a chip: Development of an integrated microfluidic platform for studying protein-ligand interactions by nuclear magnetic resonance.
University of Southampton, Doctoral Thesis, 128pp.
Record type:
Thesis
(Doctoral)
Abstract
This work demonstrates the performance of the integrated microfluidic sys tem for studying protein-ligand interactions by nuclear magnetic resonance (NMR). The platform couples together the advantages associated with microfluidic operation, i.e. minimised sample use and precision of operation, and characterisation by NMR. NMR offers unique capabilities for biomolecular research, relating to its non-invasive and non-destructive nature and atomic-scale resolution. This enables identification of the number and location of interaction sites, allosteric effects, atomic structures, dynamics of ligands and proteins, as well as full thermodynamic evaluation of the interaction. Integrating the aforementioned aspects can open new avenues for protein analysis, on one hand enhancing the usually limited throughput and functionality of NMR, on the other providing an extensive readout method to microfluidic systems, that can be fur ther linked with other analytical tools
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Published date: October 2023
Keywords:
Protein Binding, microfluidics, NMR, microfluidic-NMR
Identifiers
Local EPrints ID: 482459
URI: http://eprints.soton.ac.uk/id/eprint/482459
PURE UUID: 5764dc29-7753-4344-82ad-86a37a2b3b48
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Date deposited: 05 Oct 2023 16:46
Last modified: 12 Apr 2024 02:06
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Contributors
Author:
Marek Plata
Thesis advisor:
J.M. Werner
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