Department of Chemistry, School of Medicine, University of North Carolina, Chapel Hill, NC 27599, USA.
Phys Chem Chem Phys. 2010 Apr 14;12(14):3491-500. doi: 10.1039/b924236h.
A cell's interior is comprised of macromolecules that can occupy up to 40% of its available volume. Such crowded environments can influence the stability of proteins and their rates of reaction. Using discrete molecular dynamics simulations, we investigate how both the size and number of neighboring crowding reagents affect the thermodynamic and folding properties of structurally diverse proteins. We find that crowding induces higher compaction of proteins. We also find that folding becomes less cooperative with the introduction of crowders into the system. The crowders may induce alternative non-native protein conformations, thus creating barriers for protein folding in highly crowded media.
细胞的内部由大分子组成，这些大分子可以占据细胞内可用体积的 40%。这样拥挤的环境会影响蛋白质的稳定性及其反应速率。通过离散分子动力学模拟，我们研究了相邻拥挤试剂的大小和数量如何影响结构多样的蛋白质的热力学和折叠性质。我们发现拥挤会导致蛋白质更加紧密。我们还发现，随着向体系中引入拥挤试剂，折叠变得不那么协同。这些拥挤试剂可能会诱导蛋白质形成替代的非天然构象，从而在高度拥挤的介质中为蛋白质折叠形成障碍。
