Pulse dipolar electron paramagnetic resonance spectroscopy reveals buffer modulated cooperativity of metal templated protein dimerization

Maria Oranges, Joshua Wort, Miki Fukushima, Edoardo Fusco, Katrin Ackermann, Bela Ernest Bode*

*Corresponding author for this work

Research output: Contribution to journalLetterpeer-review

7 Citations (Scopus)
8 Downloads (Pure)

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.
Original languageEnglish
Pages (from-to)7847-7852
JournalThe Journal of Physical Chemistry Letters
Volume13
Issue number33
Early online date17 Aug 2022
DOIs
Publication statusPublished - 25 Aug 2022

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