ArticleThe journal of physical chemistry. B2015
Cysteine-specific Cu2+ chelating tags used as paramagnetic probes in double electron electron resonance.
Article in The journal of physical chemistry. B, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 49 citations in OpenAlex.
- A dynamic duo: Copper metalloregulators and continuous-wave electron spin resonance spectroscopy.Biophysical reports · 2026Review
- Rational Design of a Cu(II) Spin Label Improves the Sensitivity of Distance Measurements.The journal of physical chemistry letters · 2025Article
- A newJournal of magnetic resonance (San Diego, Calif. : 1997) · 2023Article
- The use of EPR spectroscopy to study transcription mechanisms.Biophysical reviews · 2022Review
- Article
- ESR Resolves the C Terminus Structure of the Ligand-free Human Glutathione S-Transferase A1-1.Biophysical journal · 2018Article
- A triarylmethyl spin label for long-range distance measurement at physiological temperatures using T1 relaxation enhancement.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2016Article
- Saccharides as Prospective Immobilizers of Nucleic Acids for Room-Temperature Structural EPR Studies.The journal of physical chemistry letters · 2016Article
- Distance measurements between paramagnetic ligands bound to parallel stranded guanine quadruplexes.Physical chemistry chemical physics : PCCP · 2016Article
- Rotameric preferences of a protein spin label at edge-strand β-sheet sites.Protein science : a publication of the Protein Society · 2016Article
- The double-histidine Cu²⁺-binding motif: a highly rigid, site-specific spin probe for electron spin resonance distance measurements.Angewandte Chemie (International ed. in English) · 2015Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Double electron electron resonance (DEER) is an attractive technique that is utilized for gaining insight into protein structure and dynamics via nanometer-scale distance measurements. The most commonly used paramagnetic tag in these measurements is a nitroxide spin label, R1. Here, we present the application of two types of high-affinity Cu(2+) chelating tags, based on the EDTA and cyclen metal-binding motifs as alternative X-band DEER probes, using the B1 immunoglobulin-binding domain of protein G (GB1) as a model system. Both types of tags have been incorporated into a variety of protein secondary structure environments and exhibit high spectral sensitivity. In particular, the cyclen-based tag displays distance distributions with comparable distribution widths and most probable distances within 1-3 Å when compared to homologous R1 distributions. The results display the viability of the cyclen tag as an alternative to the R1 side chain for X-band DEER distance measurements in proteins.
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