Structure of membrane embedded M13 major coat protein is insensitive to hydrophobic stress

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

Research output: Contribution to journalArticleAcademicpeer-review

9 Citations (Scopus)

Abstract

The structure of a membrane-embedded -helical reference protein, the M13 major coat protein, is characterized under different conditions of hydrophobic mismatch using fluorescence resonance energy transfer in combination with high-throughput mutagenesis. We show that the structure is similar in both thin (14:1) and thick (20:1) phospholipid bilayers, indicating that the protein does not undergo large structural rearrangements in response to conditions of hydrophobic mismatch. We introduce a "helical fingerprint" analysis, showing that amino acid residues 1¿9 are unstructured in both phospholipid bilayers. Our findings indicate the presence of -helical domains in the transmembrane segment of the protein; however, no evidence is found for a structural adaptation to the degree of hydrophobic mismatch. In light of current literature, and based on our data, we conclude that aggregation (at high protein concentration) and adjustment of the tilt angle and the lipid structure are the dominant responses to conditions of hydrophobic mismatch.
Original languageEnglish
Pages (from-to)3541-3547
JournalBiophysical Journal
Volume93
Issue number10
DOIs
Publication statusPublished - 2007

Keywords

  • lipid-bilayer
  • molecular-dynamics
  • alpha-helices
  • model
  • mismatch
  • conformation
  • modulation
  • fret
  • aggregation
  • association

Fingerprint Dive into the research topics of 'Structure of membrane embedded M13 major coat protein is insensitive to hydrophobic stress'. Together they form a unique fingerprint.

Cite this