| Autor: |
Ghosh, Shreya, Saxena, Sunil, Jeschke, Gunnar |
| Zdroj: |
Applied Magnetic Resonance; Nov2018, Vol. 49 Issue 11, p1281-1298, 18p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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