Analysis of side chain rotational restrictions of membrane-embedded

J. Strancar, A.A. Kavalenka, P. Ziherl, D. Stopar, M.A. Hemminga

Research output: Contribution to journalArticleAcademicpeer-review

4 Citations (Scopus)


Site-directed spin-labeling electron spin resonance (SDSL-ESR) is a promising tool for membrane protein structure determination. Here we propose a novel way to translate the local structural constraints gained by SDSL-ESR data into a low-resolution structure of a protein by simulating the restrictions of the local conformational spaces of the spin label attached at different protein sites along the primary structure of the membrane-embedded protein. We test the sensitivity of this approach for membrane-embedded M13 major coat protein decorated with a limited number of strategically placed spin labels employing high-throughput site-directed mutagenesis. We find a reasonably good agreement of the simulated and the experimental data taking a protein conformation close to the one determined by fluorescence resonance energy transfer analysis [P.V. Nazarov, R.B.M. Koehorst, W.L. Vos, V.V. Apanasovich, M.A. Hemminga, FRET study of membrane proteins: determination of the tilt and orientation of the N-terminal domain of M13 major coat protein, Biophys. J. 92 (2007) 1296¿1305]
Original languageEnglish
Pages (from-to)245-248
JournalJournal of Magnetic Resonance
Issue number2
Publication statusPublished - 2009


  • major coat protein
  • paramagnetic-resonance spectra
  • biosystem complexity
  • alpha-helix
  • dynamics
  • simulation
  • fret


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