Article ; Online: T
Chemical communications (Cambridge, England)
2020 Volume 56, Issue 74, Page(s) 10890–10893
Abstract: Modulating the phase-memory relaxation time (Tm) of a spin label by introducing 1H-methyl groups in a perdeuterated protein background is used in DEER experiments to assign interactions in multimodal P(r) distributions. Proof of principle is demonstrated ...
Abstract | Modulating the phase-memory relaxation time (Tm) of a spin label by introducing 1H-methyl groups in a perdeuterated protein background is used in DEER experiments to assign interactions in multimodal P(r) distributions. Proof of principle is demonstrated using Protein A where one nitroxide label occupies two distinct regions of conformational space. The presence of a single protonated methyl group in close proximity (4-8 Å) to only one of the two nitroxide rotamer ensembles results in a selective and substantial decrease in Tm, manifested by differential decay of the peak intensities in the bimodal P(r) distance distribution as a function of the total dipolar evolution time. This form of Tm filtering will facilitate DEER structural analysis of biomolecular systems with three spin labels, including complexes involving multimeric proteins. |
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MeSH term(s) | Electron Spin Resonance Spectroscopy ; Electrons ; Protons ; Spin Labels ; Staphylococcal Protein A/chemistry ; Time Factors |
Chemical Substances | Protons ; Spin Labels ; Staphylococcal Protein A |
Language | English |
Publishing date | 2020-09-16 |
Publishing country | England |
Document type | Journal Article |
ZDB-ID | 1472881-3 |
ISSN | 1364-548X ; 1359-7345 ; 0009-241X |
ISSN (online) | 1364-548X |
ISSN | 1359-7345 ; 0009-241X |
DOI | 10.1039/d0cc04369a |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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