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

Abstract : 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 (15)N-labeled protein with its unlabeled 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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Article dans une revue
Biomacromolecules, American Chemical Society, 2011, 12 (6), pp.2200-10. 〈10.1021/bm200285e〉
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https://hal-agrocampus-ouest.archives-ouvertes.fr/hal-00729257
Contributeur : Céline Martel <>
Soumis le : vendredi 7 septembre 2012 - 15:30:52
Dernière modification le : mercredi 21 mars 2018 - 16:08:07

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D.B. Salvatore, N. Duraffourg, A. Favier, B.A. Persson, M. Lund, et al.. Investigation at residue level of the early steps during the assembly of two proteins into supramolecular objects.. Biomacromolecules, American Chemical Society, 2011, 12 (6), pp.2200-10. 〈10.1021/bm200285e〉. 〈hal-00729257〉

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