Quantification of Distributions of Local Proton Concentrations in Heterogeneous Soft Matter and Non-Anfinsen Biomacromolecules
A new method to quantitatively analyze heterogeneous distributions of local proton densities around paramagnetic centers in unstructured and weakly structured biomacromolecules and soft matter is introduced, and its feasibility is demonstrated on aqueous solutions of stochastically spin-labeled poly...
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Published in | The journal of physical chemistry letters Vol. 15; no. 21; pp. 5625 - 5632 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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30.05.2024
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Abstract | A new method to quantitatively analyze heterogeneous distributions of local proton densities around paramagnetic centers in unstructured and weakly structured biomacromolecules and soft matter is introduced, and its feasibility is demonstrated on aqueous solutions of stochastically spin-labeled polysaccharides. This method is based on the pulse EPR experiment ih-RIDME (intermolecular hyperfine relaxation-induced dipolar modulation enhancement). Global analysis of a series of RIDME traces allows for a mathematically stable transformation of the time-domain data to the distribution of local proton concentrations. Two pulse sequences are proposed and tested, which combine the ih-RIDME block and the double-electron–electron resonance (DEER) experiment. Such experiments can be potentially used to correlate the local proton concentration with the macromolecular chain conformation. We anticipate an application of this approach in studies of intrinsically disordered proteins, biomolecular aggregates, and biomolecular condensates. |
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AbstractList | A new method to quantitatively
analyze heterogeneous distributions
of local proton densities around paramagnetic centers in unstructured
and weakly structured biomacromolecules and soft matter is introduced,
and its feasibility is demonstrated on aqueous solutions of stochastically
spin-labeled polysaccharides. This method is based on the pulse EPR
experiment ih-RIDME (intermolecular hyperfine relaxation-induced dipolar
modulation enhancement). Global analysis of a series of RIDME traces
allows for a mathematically stable transformation of the time-domain
data to the distribution of local proton concentrations. Two pulse
sequences are proposed and tested, which combine the ih-RIDME block
and the double-electron–electron resonance (DEER) experiment.
Such experiments can be potentially used to correlate the local proton
concentration with the macromolecular chain conformation. We anticipate
an application of this approach in studies of intrinsically disordered
proteins, biomolecular aggregates, and biomolecular condensates. A new method to quantitatively analyze heterogeneous distributions of local proton densities around paramagnetic centers in unstructured and weakly structured biomacromolecules and soft matter is introduced, and its feasibility is demonstrated on aqueous solutions of stochastically spin-labeled polysaccharides. This method is based on the pulse EPR experiment ih-RIDME (intermolecular hyperfine relaxation-induced dipolar modulation enhancement). Global analysis of a series of RIDME traces allows for a mathematically stable transformation of the time-domain data to the distribution of local proton concentrations. Two pulse sequences are proposed and tested, which combine the ih-RIDME block and the double-electron–electron resonance (DEER) experiment. Such experiments can be potentially used to correlate the local proton concentration with the macromolecular chain conformation. We anticipate an application of this approach in studies of intrinsically disordered proteins, biomolecular aggregates, and biomolecular condensates. |
Author | Wu, Xiaowen Boulos, Samy Jeschke, Gunnar Yulikov, Maxim Stolba, Dario Syryamina, Victoria N. Kuzin, Sergei Nyström, Laura |
AuthorAffiliation | Department of Health Sciences and Technology Department of Chemistry and Applied Biosciences |
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Title | Quantification of Distributions of Local Proton Concentrations in Heterogeneous Soft Matter and Non-Anfinsen Biomacromolecules |
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