Investigation at Residue Level of the Early Steps during the Assembly of Two Proteins into Supramolecular Objects

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Understanding the driving forces governing protein assembly requires the characterization of interactions at molecular level. We focus on two homologous oppositely charged proteins, lysozyme and alpha-lactalbumin, which can assemble into microspheres. The assembly early steps were characterized through the identification of interacting surfaces monitored at residue level by NMR chemical shift perturbations by titrating one N-15-labeled protein with its unlabeled partner. While a-lactalbumin has a narrow interacting site, lysozyme has interacting sites scattered on a broad surface. The further assembly of these rather unspecific heterodimers into tetrarners leads to the establishment of well-defined interaction sites. Within the tetramers, most of the electrostatic charge patches on the protein surfaces are shielded. Then, hydrophobic interactions, which are possible because alpha-lactalbumin is in a partially folded state, become preponderant, leading to the formation of larger oligomers. This approach will be particularly useful for rationalizing the design of protein assemblies as nanoscale devices.


  • Delphine B. Salvatore
  • Nicolas Duraffourg
  • Adrien Favier
  • Björn Persson
  • Mikael Lund
  • Marie-Madeleine Delage
  • Robert Silvers
  • Harald Schwalbe
  • Thomas Croguennec
  • Said Bouhallab
  • Vincent Forge
Enheter & grupper

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Teoretisk kemi
Sidor (från-till)2200-2210
StatusPublished - 2011
Peer review utfördJa