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Journal/Book: Biomacromolecules
Published: 2011
Pages: 2200-2210
Volume: 12
Issue: 6
Accession no.:

Investigation at residue level of the early steps during the assembly of two proteins into supramolecular objects

Delphine B. Salvatore, Nicolas Duraffourg, Adrien Favier, Björn A. Persson, Mikael Lund, Marie-Madeleine Delage, Robert Silvers, Harald Schwalbe, Thomas Croguennec, Saïd Bouhallab, Vincent Forge
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 α-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 15N-labelled protein with its unlabelled partner. While α-lactalbumin has a narrow interacting site, lysozyme has interacting sites scattered on a broad surface. The further assembly of these rather unspecific heterodimers into tetramers 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 α-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.
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Prof. Dr. Harald Schwalbe
Institut für Organische Chemie und Chemische Biologie
Johann Wolfgang Goethe Universität
Max-von-Laue-Str. 7
D-60438 Frankfurt am Main
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