From "I" to "L" and back again: the odyssey of membrane-bound M13 protein

W.L. Vos, P.V. Nazarov, R.B.M. Koehorst, R.B. Spruijt, M.A. Hemminga

Research output: Contribution to journalArticleAcademicpeer-review

17 Citations (Scopus)


The major coat protein of the filamentous bacteriophage M13 is a surprising protein because it exists both as a membrane protein and as part of the M13 phage coat during its life cycle. Early studies showed that the phage-bound structure of the coat protein was a continuous I-shaped ¿-helix. However, throughout the years various structural models, both I-shaped and L-shaped, have been proposed for the membrane-bound state of the coat protein. Recently, site-directed labelling approaches have enabled the study of the coat protein under conditions that more closely mimic the in vivo membrane-bound state. Interestingly, the structure that has emerged from this work is I-shaped and similar to the structure in the phage-bound state
Original languageEnglish
Pages (from-to)249-255
JournalTrends in Biochemical Sciences
Issue number5
Publication statusPublished - 2009


  • major coat protein
  • amino-acids
  • filamentous bacteriophages
  • nmr-spectroscopy
  • fd
  • dynamics
  • domain
  • helix
  • environments
  • resolution


Dive into the research topics of 'From "I" to "L" and back again: the odyssey of membrane-bound M13 protein'. Together they form a unique fingerprint.

Cite this