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MeSH Review

Electron Spin Resonance Spectroscopy

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Disease relevance of Electron Spin Resonance Spectroscopy


Psychiatry related information on Electron Spin Resonance Spectroscopy


High impact information on Electron Spin Resonance Spectroscopy


Chemical compound and disease context of Electron Spin Resonance Spectroscopy


Biological context of Electron Spin Resonance Spectroscopy


Anatomical context of Electron Spin Resonance Spectroscopy


Associations of Electron Spin Resonance Spectroscopy with chemical compounds

  • Electron paramagnetic resonance (EPR) measurements of nitroxide-labeled peptides provided intersubunit distance measurements that also supported the parallel model [29].
  • In the presence of RTPR containing specifically deuterated cysteine residues, the electron paramagnetic resonance (EPR) spectrum of an intermediate in the exchange reaction and the reduction reaction, trapped by rapid freeze quench techniques, exhibits narrowed hyperfine features relative to the corresponding unlabeled RTPR [30].
  • Electron paramagnetic resonance and optical spectroscopic experiments indicated that the salivary vasodilator is a nitrosylheme protein with an Fe(III) heme that binds nitric oxide (NO) reversibly [31].
  • Low-temperature 35-gigahertz (Q-band) electron nuclear double resonance (ENDOR) spectroscopy was used to examine compound ES prepared from proteins containing specifically deuterated methionine or tryptophan, as well as the amino acid replacement Trp51----Phe [32].
  • The relative collision frequency of each spin label with freely diffusing oxygen and membrane-impermeant chromium oxalate was estimated with power saturation EPR (electron paramagnetic resonance) spectroscopy [33].

Gene context of Electron Spin Resonance Spectroscopy


Analytical, diagnostic and therapeutic context of Electron Spin Resonance Spectroscopy


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