Membrane assembly of M13 major coat protein: evidence for a structural adaptation in the hinge region and a tilted transmembrane domain.

@article{Spruijt2004MembraneAO,
  title={Membrane assembly of M13 major coat protein: evidence for a structural adaptation in the hinge region and a tilted transmembrane domain.},
  author={Ruud B. Spruijt and Cor J. A. M. Wolfs and Marcus A. Hemminga},
  journal={Biochemistry},
  year={2004},
  volume={43 44},
  pages={13972-80}
}
New insights into the low-resolution structure of the hinge region and the transmembrane domain of the membrane-bound major coat protein of the bacteriophage M13 are deduced from a single cysteine-scanning approach using fluorescence spectroscopy. New mutant coat proteins are labeled and reconstituted into phospholipid bilayers with varying headgroup compositions (PC, PE, and PG) and thicknesses (14:1PC, 18:1PC, and 22:1PC). Information about the polarity of the local environment around the… CONTINUE READING
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