Going the dHis-tance: Site-Directed Cu2+ Labeling of Proteins and Nucleic Acids
Author:
Affiliation:
1. Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States
Funder
Division of Molecular and Cellular Biosciences
Publisher
American Chemical Society (ACS)
Subject
General Medicine,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.accounts.0c00761
Reference84 articles.
1. Cu2+-based distance measurements by pulsed EPR provide distance constraints for DNA backbone conformations in solution
2. Double Histidine Based EPR Measurements at Physiological Temperatures Permit Site‐Specific Elucidation of Hidden Dynamics in Enzymes
3. Molecular Dynamics Simulations Based on Newly Developed Force Field Parameters for Cu2+ Spin Labels Provide Insights into Double-Histidine-Based Double Electron–Electron Resonance
4. The Double-Histidine Cu2+-Binding Motif: A Highly Rigid, Site-Specific Spin Probe for Electron Spin Resonance Distance Measurements
5. The Development of High-Field /High Frequency ESR
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