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

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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; Lund, Mikael; Delage, Marie-Madeleine; Silvers, Robert; Schwalbe, Harald; Croguennec, Thomas; Bouhallab, Said; Forge, Vincent.

In: Biomacromolecules, Vol. 12, No. 6, 2011, p. 2200-2210.

Research output: Contribution to journalArticle

Harvard

Salvatore, DB, Duraffourg, N, Favier, A, Persson, B, Lund, M, Delage, M-M, Silvers, R, Schwalbe, H, Croguennec, T, Bouhallab, S & Forge, V 2011, 'Investigation at Residue Level of the Early Steps during the Assembly of Two Proteins into Supramolecular Objects', Biomacromolecules, vol. 12, no. 6, pp. 2200-2210. https://doi.org/10.1021/bm200285e

APA

CBE

Salvatore DB, Duraffourg N, Favier A, Persson B, Lund M, Delage M-M, Silvers R, Schwalbe H, Croguennec T, Bouhallab S, Forge V. 2011. Investigation at Residue Level of the Early Steps during the Assembly of Two Proteins into Supramolecular Objects. Biomacromolecules. 12(6):2200-2210. https://doi.org/10.1021/bm200285e

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Author

Salvatore, Delphine B. ; Duraffourg, Nicolas ; Favier, Adrien ; Persson, Björn ; Lund, Mikael ; Delage, Marie-Madeleine ; Silvers, Robert ; Schwalbe, Harald ; Croguennec, Thomas ; Bouhallab, Said ; Forge, Vincent. / Investigation at Residue Level of the Early Steps during the Assembly of Two Proteins into Supramolecular Objects. In: Biomacromolecules. 2011 ; Vol. 12, No. 6. pp. 2200-2210.

RIS

TY - JOUR

T1 - Investigation at Residue Level of the Early Steps during the Assembly of Two Proteins into Supramolecular Objects

AU - Salvatore, Delphine B.

AU - Duraffourg, Nicolas

AU - Favier, Adrien

AU - Persson, Björn

AU - Lund, Mikael

AU - Delage, Marie-Madeleine

AU - Silvers, Robert

AU - Schwalbe, Harald

AU - Croguennec, Thomas

AU - Bouhallab, Said

AU - Forge, Vincent

N1 - 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)

PY - 2011

Y1 - 2011

N2 - 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.

AB - 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.

U2 - 10.1021/bm200285e

DO - 10.1021/bm200285e

M3 - Article

VL - 12

SP - 2200

EP - 2210

JO - Biomacromolecules

T2 - Biomacromolecules

JF - Biomacromolecules

SN - 1526-4602

IS - 6

ER -