ArticleAngewandte Chemie (International ed. in English)2015
The double-histidine Cu²⁺-binding motif: a highly rigid, site-specific spin probe for electron spin resonance distance measurements.
Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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68 citing papers in PubMed, 169 citations in OpenAlex.
- Binding Affinity Determines the Success of Endogenous CuThe journal of physical chemistry letters · 2026Article
- A dynamic duo: Copper metalloregulators and continuous-wave electron spin resonance spectroscopy.Biophysical reports · 2026Review
- Large-scale protein conformational transitions revealed by weighted ensemble simulations and EPR.Chemical science · 2026Article
- Advances in EPR Approaches for Studying Structural Properties of Membrane Proteins.Magnetic resonance in chemistry : MRC · 2026Review
- Rational Design of a Cu(II) Spin Label Improves the Sensitivity of Distance Measurements.The journal of physical chemistry letters · 2025Article
- BR-bodies facilitate adaptive responses and survival during copper stress in Caulobacter crescentus.The Journal of biological chemistry · 2025Article
- Q-Band Double Quantum Coherence ESR for Sensitive Nitroxide-Based Distance Measurements.The journal of physical chemistry. B · 2025Article
- Effect of Hydrostatic Pressure on theThe journal of physical chemistry letters · 2025Article
- Caught in the Middle: A Rigid DNA Label That Provides an Incisive Picture of DNA Conformational Flexibility in Protein-DNA Complexes.Journal of the American Chemical Society · 2025Article
- Protein Modeling with DEER Spectroscopy.Annual review of biophysics · 2025Review
- BR-Bodies Facilitate Adaptive Responses and Survival During Copper Stress inbioRxiv : the preprint server for biology · 2025Article
- Exploring the Gating Mechanism of the Human Copper Transporter, hCtr1, Using EPR Spectroscopy.Biomolecules · 2025Article
- Endogenous Cu(II) Labeling for Distance Measurements on Proteins by EPR.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- Pulsed EPR Methods in the Angstrom to Nanometre Scale Shed Light on the Conformational Flexibility of a Fluoride Riboswitch.Angewandte Chemie (International ed. in English) · 2024Article
- Tracking Disordered Extracellular Domains of Membrane Proteins in the Cell with Cu(II)-Based Spin Labels.The journal of physical chemistry. B · 2024Article
- EPR spectroscopic characterisation of native CuDalton transactions (Cambridge, England : 2003) · 2024Article
- Xplor-NIH: Better parameters and protocols for NMR protein structure determination.Protein science : a publication of the Protein Society · 2024Article
- Modeling of Cu(II)-based protein spin labels using rotamer libraries.Physical chemistry chemical physics : PCCP · 2024Article
- Pulse Dipolar Electron Paramagnetic Resonance Spectroscopy Distance Measurements at Low Nanomolar Concentrations: The CuThe journal of physical chemistry letters · 2024Article
- The chromatin remodeler SMARCA5 binds to d-block metal supports: Characterization of affinities by IMAC chromatography and QM analysis.PloS one · 2024Article
8 more citing papers are in PubMed but not listed here.
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5 authors at 1 institution in 1 country.
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Abstract
The development of ESR methods that measure long-range distance distributions has advanced biophysical research. However, the spin labels commonly employed are highly flexible, which leads to ambiguity in relating ESR measurements to protein-backbone structure. Herein we present the double-histidine (dHis) Cu(2+)-binding motif as a rigid spin probe for double electron-electron resonance (DEER) distance measurements. The spin label is assembled in situ from natural amino acid residues and a metal salt, requires no postexpression synthetic modification, and provides distance distributions that are dramatically narrower than those found with the commonly used protein spin label. Simple molecular modeling based on an X-ray crystal structure of an unlabeled protein led to a predicted most probable distance within 0.5 Å of the experimental value. Cu(2+) DEER with the dHis motif shows great promise for the resolution of precise, unambiguous distance constraints that relate directly to protein-backbone structure and flexibility.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.