ArticleJournal of the American Chemical Society2014
Long-range distance measurements in proteins at physiological temperatures using saturation recovery EPR spectroscopy.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 48 citations in OpenAlex.
- Advances in EPR Approaches for Studying Structural Properties of Membrane Proteins.Magnetic resonance in chemistry : MRC · 2026Review
- Determination of absolute intramolecular distances in proteins using anomalous X-ray scattering interferometry.Nanoscale · 2025Article
- RIDME Spectroscopy: New Topics Beyond the Determination of Electron Spin-Spin Distances.The journal of physical chemistry letters · 2025Review
- A pressure-jump EPR system to monitor millisecond conformational exchange rates of spin-labeled proteins.Protein science : a publication of the Protein Society · 2024Article
- A pressure-jump EPR system to monitor millisecond conformational exchange rates of spin-labeled proteins.bioRxiv : the preprint server for biology · 2024Article
- A Highly Ordered Nitroxide Side Chain for Distance Mapping and Monitoring Slow Structural Fluctuations in Proteins.Applied magnetic resonance · 2024Article
- Cucurbit[7]uril Enhances Distance Measurements of Spin-Labeled Proteins.Journal of the American Chemical Society · 2023Article
- Protocol for resolving enzyme orientation and dynamics in advanced porous materials via SDSL-EPR.STAR protocols · 2021Article
- Different Single-Enzyme Conformational Dynamics upon Binding Hydrolyzable or Nonhydrolyzable Ligands.The journal of physical chemistry. B · 2021Article
- DEER Analysis of GPCR Conformational Heterogeneity.Biomolecules · 2021Review
- Ox-SLIM: Synthesis of and Site-Specific Labelling with a Highly Hydrophilic Trityl Spin Label.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Metal-Organic Frameworks for Enzyme Immobilization: Beyond Host Matrix Materials.ACS central science · 2020Review
- Protein Detection using Quadratic Fit Analysis Near Dirac Point of Graphene Field Effect Biosensors.ACS applied electronic materials · 2020Article
- Insights on the Structure, Molecular Weight and Activity of an Antibacterial Protein-Polymer Hybrid.Chemphyschem : a European journal of chemical physics and physical chemistry · 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
- Pulsed EPR characterization of HIV-1 protease conformational sampling and inhibitor-induced population shifts.Physical chemistry chemical physics : PCCP · 2016Article
- Development of electron spin echo envelope modulation spectroscopy to probe the secondary structure of recombinant membrane proteins in a lipid bilayer.Protein science : a publication of the Protein Society · 2015Article
- Room-Temperature Electron Spin Relaxation of Triarylmethyl Radicals at the X- and Q-Bands.The journal of physical chemistry. B · 2015Article
- 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
6 authors at 2 institutions in 1 country.
Funding
Abstract
Site-directed spin labeling in combination with EPR is a powerful method for providing distances on the nm scale in biological systems. The most popular strategy, double electron-electron resonance (DEER), is carried out at cryogenic temperatures (50-80 K) to increase the short spin-spin relaxation time (T2) upon which the technique relies. A challenge is to measure long-range distances (20-60 Å) in proteins near physiological temperatures. Toward this goal we are investigating an alternative approach based on the distance-dependent enhancement of spin-lattice relaxation rate (T1(-1)) of a nitroxide spin label by a paramagnetic metal. With a commonly used nitroxide side chain (R1) and Cu(2+), it has been found that interspin distances ≤25 Å can be determined in this way (Jun et al. Biochemistry 2006, 45, 11666). Here, the upper limit of the accessible distance is extended to ≈40 Å using spin labels with long T1, a high-affinity 5-residue Cu(2+) binding loop inserted into the protein sequence, and pulsed saturation recovery to measure relaxation enhancement. Time-domain Cu(2+) electron paramagnetic resonance, quantum mechanical calculations, and molecular dynamics simulations provide information on the structure and geometry of the Cu(2+) loop and indicate that the metal ion is well-localized in the protein. An important aspect of these studies is that both Cu(2+)/nitroxide DEER at cryogenic temperatures and T1 relaxation measurements at room temperature can be carried out on the same sample, allowing both validation of the relaxation method and assessment of the effect of freezing on protein structure.
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