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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.
https://hal-agrocampus-ouest.archives-ouvertes.fr/hal-00729257
Contributor : Céline Martel Connect in order to contact the contributor
Submitted on : Friday, September 7, 2012 - 3:30:52 PM
Last modification on : Wednesday, April 6, 2022 - 4:08:11 PM
Contributor : Céline Martel Connect in order to contact the contributor
Submitted on : Friday, September 7, 2012 - 3:30:52 PM
Last modification on : Wednesday, April 6, 2022 - 4:08:11 PM