Motional restrictions of membrane proteins: a site-directed spin labeling study

D. Stopar, J. Strancar, R.B. Spruijt, M.A. Hemminga

Research output: Contribution to journalArticleAcademicpeer-review

25 Citations (Scopus)


Site-directed mutagenesis was used to produce 27 single cysteine mutants of bacteriophage M13 major coat protein spanning the whole primary sequence of the protein. Single-cysteine mutants were labeled with nitroxide spin labels and incorporated into phospholipid bilayers with increasing acyl chain length. The SDSL is combined with ESR and CD spectroscopy. CD spectroscopy provided information about the overall protein conformation in different mismatching lipids. The spin label ESR spectra were analyzed in terms of a new spectral simulation approach based on hybrid evolutionary optimization and solution condensation. This method gives the residue-level free rotational space (i.e., the effective space within which the spin label can wobble) and the diffusion constant of the spin label attached to the protein. The results suggest that the coat protein has a large structural flexibility, which facilitates a stable protein-to-membrane association in lipid bilayers with various degrees of hydrophobic mismatch.
Original languageEnglish
Pages (from-to)3341-3348
Number of pages8
JournalBiophysical Journal
Issue number9
Publication statusPublished - 2006


  • major coat protein
  • bacteriophage m13
  • transmembrane domain
  • biological-membranes
  • biosystem complexity
  • lipid interactions
  • epr
  • dynamics
  • residues
  • systems

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