Advanced EPR spectroscopy for investigation of biomolecular binding events

Wort, Joshua L.; Oranges, Maria; Ackermann, Katrin; Bode, Bela E.

doi:10.1039/9781839162534-00047

Cited by 2 publications

(3 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“… 16 Moreover, PDS has recently emerged as an excellent complementary tool for studying metal ion binding equilibria with submicromolar sensitivity. 17 − 21 …”

mentioning

confidence: 99%

“…Several techniques such as X-ray crystallography, nuclear magnetic resonance (NMR), and sedimentation velocity have extensively characterized these binding processes. ,, Pulse dipolar electron paramagnetic resonance spectroscopy (PDS) has been employed to characterize metal motifs that induce polymerization and the conformational flexibility of supramolecular polymers . Moreover, PDS has recently emerged as an excellent complementary tool for studying metal ion binding equilibria with submicromolar sensitivity. − …”

mentioning

confidence: 99%

See 1 more Smart Citation

Pulse Dipolar Electron Paramagnetic Resonance Spectroscopy Reveals Buffer-Modulated Cooperativity of Metal-Templated Protein Dimerization

Oranges

Wort

Fukushima

et al. 2022

J. Phys. Chem. Lett.

Self Cite

View full text Add to dashboard Cite

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 Cu II -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 Cu II 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.

show abstract

“… 16 Moreover, PDS has recently emerged as an excellent complementary tool for studying metal ion binding equilibria with submicromolar sensitivity. 17 − 21 …”

mentioning

confidence: 99%

mentioning

confidence: 99%

Pulse Dipolar Electron Paramagnetic Resonance Spectroscopy Reveals Buffer-Modulated Cooperativity of Metal-Templated Protein Dimerization

Oranges

Wort

Fukushima

et al. 2022

J. Phys. Chem. Lett.

Self Cite

View full text Add to dashboard Cite

show abstract

“…5,7,14 Dipolar electron paramagnetic resonance (EPR) spectroscopy has recently emerged as an excellent complementary tool for studying metal ion-binding equilibria with sub-micromolar sensitivity. [15][16][17][18][19] The four-pulse DEER [20][21][22] (double electron-electron resonance) and the five-pulse RIDME 23,24 (relaxation-induced dipolar modulation enhancement) experiments (for pulse sequences see ESI section 1.3) allow detection of the weak dipolar interaction between paramagnetic centres, which is characterized by modulation with the dipolar frequency (ωAB) that encodes the inter-spin distance, rAB. The modulation depth (Δ) of these traces (i.e., the amplitude between the signal intensity at 𝑡 = 0 and the time when the signal is entirely damped in the limit of negligible intermolecular decay) informs the number of coupled spins.…”

mentioning

confidence: 99%

Pulse dipolar EPR spectroscopy reveals buffer modulated cooperativity of metal templated protein dimerization

Oranges

Wort

Fukushima

et al. 2022

Preprint

Self Cite

View full text Add to dashboard Cite

Self-assembly of protein monomers directed by metal ion coordination constitutes a promising strategy for designing supramolecular architectures complicated by the non-covalent interaction between monomers. Herein, two pulse dipolar electron paramagnetic resonance spectroscopy (PDS) techniques, double electron-electron resonance (DEER) and relaxation-induced dipolar modulation enhancement (RIDME), were simultaneously employed for studying 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 cooperativity of protein dimerization across α-helical double-histidine motifs in presence of Cu(II) is strongly buffer modulated, 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.

show abstract

Advanced EPR spectroscopy for investigation of biomolecular binding events

Cited by 2 publications

References 0 publications

Pulse Dipolar Electron Paramagnetic Resonance Spectroscopy Reveals Buffer-Modulated Cooperativity of Metal-Templated Protein Dimerization

Pulse Dipolar Electron Paramagnetic Resonance Spectroscopy Reveals Buffer-Modulated Cooperativity of Metal-Templated Protein Dimerization

Pulse dipolar EPR spectroscopy reveals buffer modulated cooperativity of metal templated protein dimerization

Contact Info

Product

Resources

About