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

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Bibtex

@article{2d4971fec16a4898b4cdf13cfc0c36a4,
title = "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 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.",
author = "Salvatore, {Delphine B.} and Nicolas Duraffourg and Adrien Favier and Bj{\"o}rn Persson and Mikael Lund and Marie-Madeleine Delage and Robert Silvers and Harald Schwalbe and Thomas Croguennec and Said Bouhallab and Vincent Forge",
note = "The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)",
year = "2011",
doi = "10.1021/bm200285e",
language = "English",
volume = "12",
pages = "2200--2210",
journal = "Biomacromolecules",
issn = "1526-4602",
publisher = "The American Chemical Society (ACS)",
number = "6",

}