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Article

Copper-based pulsed dipolar ESR spectroscopy as a probe of protein conformation linked to disease states.

Biophysical journal - 7 Oct 2014

Merz Gregory E, Borbat Peter P, Pratt Ashley J, Getzoff Elizabeth D, Freed Jack H, Crane Brian R

Abstract excerpt

We demonstrate the ability of pulsed dipolar electron spin resonance (ESR) spectroscopy (PDS) to report on the conformation of Cu-Zn superoxide dismutase (SOD1) through the sensitive measurement of dipolar interactions between inherent Cu(2+) ions. Although the extent and the anisotropy of the Cu ESR spectrum provides challenges for PDS, Ku-band (17.3 GHz) double electron-electron resonance and double-quantum...

Topics

Amyotrophic Lateral Sclerosis
Copper
Crystallography, X-Ray
Disease Progression
Electron Spin Resonance Spectroscopy
Humans
Models, Molecular
Mutation
Protein Binding
Protein Multimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Structure, Quaternary

Superoxide Dismutase

Source

Open in PubMed Open full text

Identifiers

PMID: 25296320
DOI: 10.1016/j.bpj.2014.07.068
PMCID: PMC4190658

Genes

SOD1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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