化学
溶菌酶
超分子化学
残留物(化学)
自组装
生物物理学
乳清蛋白
静电学
静电
蛋白质结构
疏水效应
结晶学
生物化学
有机化学
物理化学
电气工程
工程类
晶体结构
生物
作者
Delphine Salvatore,Nicolas Duraffourg,Adrien Favier,Björn Persson,Mikael Lund,Marie-Madeleine Delage,Robert Silvers,Harald Schwalbe,Thomas Croguennec,Saı̈d Bouhallab,Vincent Forge
出处
期刊:Biomacromolecules
[American Chemical Society]
日期:2011-05-13
卷期号:12 (6): 2200-2210
被引量:18
摘要
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 15N-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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