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Pulse dipolar electron paramagnetic resonance spectroscopy reveals buffer modulated cooperativity of metal templated protein dimerization
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dc.contributor.author | Oranges, Maria | |
dc.contributor.author | Wort, Joshua | |
dc.contributor.author | Fukushima, Miki | |
dc.contributor.author | Fusco, Edoardo | |
dc.contributor.author | Ackermann, Katrin | |
dc.contributor.author | Bode, Bela Ernest | |
dc.date.accessioned | 2022-08-18T15:30:04Z | |
dc.date.available | 2022-08-18T15:30:04Z | |
dc.date.issued | 2022-08-25 | |
dc.identifier | 280815925 | |
dc.identifier | 777adc89-6959-4e00-bae5-11f6364dbd60 | |
dc.identifier | 85136610075 | |
dc.identifier | 000845073700001 | |
dc.identifier.citation | Oranges , M , Wort , J , Fukushima , M , Fusco , E , Ackermann , K & Bode , B E 2022 , ' Pulse dipolar electron paramagnetic resonance spectroscopy reveals buffer modulated cooperativity of metal templated protein dimerization ' , The Journal of Physical Chemistry Letters , vol. 13 , no. 33 , pp. 7847-7852 . https://doi.org/10.1021/acs.jpclett.2c01719 | en |
dc.identifier.issn | 1948-7185 | |
dc.identifier.other | ORCID: /0000-0002-3384-271X/work/117997006 | |
dc.identifier.uri | https://hdl.handle.net/10023/25861 | |
dc.description | Funding: Leverhulme Trust - RPG-2018397; Biotechnology and Biological Sciences Research Council - BB/M010996/1; Engineering and Physical Sciences Research Council - EP/N509759/1; Wellcome Trust - 204821/Z/16/Z. | en |
dc.description.abstract | Self-assembly of protein monomers directed by metal ion coordination constitutes a promising strategy for designing supramolecular architectures complicated by the noncovalent interaction between monomers. Herein, two pulse dipolar electron paramagnetic resonance spectroscopy (PDS) techniques, pulse electron–electron double resonance and relaxation-induced dipolar modulation enhancement, were simultaneously employed to study the CuII-templated dimerization behavior of a model protein (Streptococcus sp. group G, protein G B1 domain) in both phosphate and Tris-HCl buffers. A cooperative binding model could simultaneously fit all data and demonstrate that the cooperativity of protein dimerization across α-helical double-histidine motifs in the presence of CuII is strongly modulated by the buffer, representing a platform for highly tunable buffer-switchable templated dimerization. Hence, PDS enriches the family of techniques for monitoring binding processes, supporting the development of novel strategies for bioengineering structures and stable architectures assembled by an initial metal-templated dimerization. | |
dc.format.extent | 2551990 | |
dc.language.iso | eng | |
dc.relation.ispartof | The Journal of Physical Chemistry Letters | en |
dc.subject | QD Chemistry | en |
dc.subject | DAS | en |
dc.subject.lcc | QD | en |
dc.title | Pulse dipolar electron paramagnetic resonance spectroscopy reveals buffer modulated cooperativity of metal templated protein dimerization | en |
dc.type | Journal item | en |
dc.contributor.sponsor | The Leverhulme Trust | en |
dc.contributor.sponsor | BBSRC | en |
dc.contributor.sponsor | BBSRC | en |
dc.contributor.sponsor | The Wellcome Trust | en |
dc.contributor.institution | University of St Andrews. School of Chemistry | en |
dc.contributor.institution | University of St Andrews. Institute of Behavioural and Neural Sciences | en |
dc.contributor.institution | University of St Andrews. EaSTCHEM | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.contributor.institution | University of St Andrews. Centre of Magnetic Resonance | en |
dc.identifier.doi | 10.1021/acs.jpclett.2c01719 | |
dc.description.status | Peer reviewed | en |
dc.identifier.grantnumber | RPG-2018-397 | en |
dc.identifier.grantnumber | BB/T017740/1 | en |
dc.identifier.grantnumber | BB/R013780/1 | en |
dc.identifier.grantnumber | N/A | en |
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