Rotamer Modelling of Cu(II) Spin Labels Based on the Double-Histidine Motif
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Date
2018-11
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Journal Article
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Abstract
Spin labels attached to two residues of a protein chain have less conformational flexibility than those attached to a single residue and thus lead to a narrower spatial distribution of the unpaired electron. The case of Cu²⁺ labels based on the double-histidine (dHis) motif is of particular interest, as it combines the advantage of precise localization of the unpaired electron with a labelling scheme orthogonal to the more common cysteine-based labelling. Here, we introduce an approach for in silico spin labelling of a protein by dHis motifs and Cu²⁺ complexes of iminodiacetic acid or nitrilotriacetic acid. We discuss a computerized scan for native histidine pairs that might be prone to bind such Cu²⁺ complexes and spin-labelling site pair scans that can identify suitable double mutants for labelling. Predicted distance distributions between two Cu²⁺ labels are compared to experimental distance distributions. We also test the hypothesis that elastic network modelling of conformational transitions with Cu²⁺-dHis labels can provide more accurate structural models than with nitroxide labels.
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published
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49 (11)
Pages / Article No.
1281 - 1298
Publisher
Springer
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03810 - Jeschke, Gunnar / Jeschke, Gunnar
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It was possible to publish this article open access thanks to a Swiss National Licence with the publisher.
Funding
169057 - Generation of spin-label based restraints on biomolecular structure and their use in hybrid structure modelling (SNF)