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

Salvatore, Delphine B.; Duraffourg, Nicolas; Favier, Adrien; Persson, Björn LU ; Lund, Mikael LU ; Delage, Marie-Madeleine; Silvers, Robert; Schwalbe, Harald; Croguennec, Thomas and Bouhallab, Said, et al. (2011) In Biomacromolecules 12(6). p.2200-2210
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,... (More)
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. (Less)
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published
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Biomacromolecules
volume
12
issue
6
pages
2200 - 2210
publisher
The American Chemical Society
external identifiers
  • wos:000291499900029
  • scopus:79958842162
ISSN
1526-4602
DOI
10.1021/bm200285e
language
English
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yes
id
2d4971fe-c16a-4898-b4cd-f13cfc0c36a4 (old id 2056826)
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2011-07-26 10:20:36
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2017-07-23 03:03:03
@article{2d4971fe-c16a-4898-b4cd-f13cfc0c36a4,
  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 Duraffourg, Nicolas and Favier, Adrien and Persson, Björn and Lund, Mikael and Delage, Marie-Madeleine and Silvers, Robert and Schwalbe, Harald and Croguennec, Thomas and Bouhallab, Said and Forge, Vincent},
  issn         = {1526-4602},
  language     = {eng},
  number       = {6},
  pages        = {2200--2210},
  publisher    = {The American Chemical Society},
  series       = {Biomacromolecules},
  title        = {Investigation at Residue Level of the Early Steps during the Assembly of Two Proteins into Supramolecular Objects},
  url          = {http://dx.doi.org/10.1021/bm200285e},
  volume       = {12},
  year         = {2011},
}