Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The global analysis of DEER data.

Journal of magnetic resonance (San Diego, Calif. : 1997) - 1 May 2012

Brandon Suzanne, Beth Albert H, Hustedt Eric J

Abstract excerpt

Double Electron-Electron Resonance (DEER) has emerged as a powerful technique for measuring long range distances and distance distributions between paramagnetic centers in biomolecules. This information can then be used to characterize functionally relevant structural and dynamic properties of biological molecules and their macromolecular assemblies. Approaches have been developed for analyzing experimental data...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Data Interpretation, Statistical
Share to Muramidase
Share to Normal Distribution

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cysteine

Share to Computer Simulation

Share to Confidence Intervals

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Spin Labels

Source

Open in PubMed Open full text

Identifiers

PMID: 22578560
DOI: 10.1016/j.jmr.2012.03.006
PMCID: PMC3608411

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 11 closest

The global analysis of DEER data.PMID 22578560Read ↗

Effect of freezing conditions on distances and their distributions derived from Double Electron Electron Resonance (DEER): a study of doubly-spin-labeled T4 lysozyme.Semantic proximity Read ↗

Orthogonal spin labeling and Gd(III)-nitroxide distance measurements on bacteriophage T4-lysozyme.Semantic proximity Read ↗

Inter-spin distance determination using L-band (1-2 GHz) non-adiabatic rapid sweep electron paramagnetic resonance (NARS EPR).Semantic proximity Read ↗

Determining the oligomeric structure of proteorhodopsin by Gd3+ -based pulsed dipolar spectroscopy of multiple distances.Semantic proximity Read ↗

Long-range distance measurements in proteins at physiological temperatures using saturation recovery EPR spectroscopy.Semantic proximity Read ↗

Simultaneous measurement of 1HC/N-R2's for rapid acquisition of backbone and sidechain paramagnetic relaxation enhancements (PREs) in proteins.Semantic proximity Read ↗

Gadolinium tagging for high-precision measurements of 6 nm distances in protein assemblies by EPR.Semantic proximity Read ↗

Monomeric and dimeric conformation of the vinculin tail five-helix bundle in solution studied by EPR spectroscopy.Semantic proximity Read ↗

Assessing induced folding of an intrinsically disordered protein by site-directed spin-labeling electron paramagnetic resonance spectroscopy.Semantic proximity Read ↗

Long distance PELDOR measurements on the histone core particle.Semantic proximity Read ↗

Solution NMR investigation of the CD95/FADD homotypic death domain complex suggests lack of engagement of the CD95 C terminus.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.