Structural studies on membrane proteins using non-linear spin label EPR spectroscopy

T. Páli, Derek Marsh

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Non-linear electron spin resonance (EPR) techniques suitable for measuring- proximity relationships in membranes are reviewed. These were developed during the past decade in order to measure changes sensitively in the spin-lattice relaxation time (T1) of nitroxyl spin labels covalently attached to membrane lipids or proteins. In combination with paramagnetic quenching agents and double spin-labelling, the methods were further developed for distance measurements. Selected examples are given to illustrate different methods, and types of data obtained for both integral and peripheral membrane proteins.

Original languageEnglish
Pages (from-to)87-91
Number of pages5
JournalCellular and Molecular Biology Letters
Volume7
Issue number1
Publication statusPublished - 2002

Fingerprint

Electron spin resonance spectroscopy
Spin Labels
Electron Spin Resonance Spectroscopy
Membrane Proteins
Distance measurement
Spin-lattice relaxation
Membrane Lipids
Relaxation time
Labeling
Paramagnetic resonance
Quenching
Membranes
nitroxyl

Keywords

  • Electron paramagnetic resonance
  • Membrane protein
  • Microwave saturation
  • Saturation transfer
  • Site directed spin labelling
  • Spin label
  • Spin-spin interaction

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Structural studies on membrane proteins using non-linear spin label EPR spectroscopy. / Páli, T.; Marsh, Derek.

In: Cellular and Molecular Biology Letters, Vol. 7, No. 1, 2002, p. 87-91.

Research output: Contribution to journalArticle

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