Influence of crowded cellular environments on protein folding, binding, and oligomerization: biological consequences and potentials of atomistic modeling.
Influence of crowded cellular environments on protein folding, binding, and oligomerization: biological consequences and potentials of atomistic modeling.
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DOI：
10.1016/j.febslet.2013.01.064
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发表时间：
2013-04-17
期刊：
影响因子：
3.5
通讯作者：
Zhou HX
中科院分区：
文献类型：
--
作者：
Zhou HX
最近在细胞内和细胞模拟条件下的实验表明，在其中发现的拥挤环境可以显着重塑单个蛋白质分子及其寡聚体的能量景观。由此产生的构象和寡聚状态的群体的变化具有许多生物学后果，包括复制和转录的效率、聚集相关疾病的发展以及小分子药物的功效。一些拥挤的影响，可以从硬颗粒理论模型，但在体外和体内的测量表明，这些影响往往是微妙和复杂的。这些观察，再加上最近的计算研究在原子水平上，表明后者的详细建模可能需要产生的拥挤的细胞环境的影响的定量理解。
Recent experiments inside cells and in cytomimetic conditions have demonstrated that the crowded environments found therein can significantly reshape the energy landscapes of individual protein molecules and their oligomers. The resulting shifts in populations of conformational and oligomeric states have numerous biological consequences, including on the efficiency of replication and transcription, the development of aggregation-related diseases, and the efficacy of small-molecule drugs. Some of the effects of crowding can be anticipated from hard-particle theoretical models, but the in vitro and in vivo measurements indicate that these effects are often subtle and complex. These observations, coupled with recent computational studies at the atomistic level, suggest that the latter detailed modeling may be required to yield a quantitative understanding on the influences of the crowded cellular environments.