Protein folding and protein design has become one of the most actively studied problems in modern molecular biology.
蛋白质折叠和蛋白质设计的研究是当代分子生物学的热点问题，具有重要的科学意义。
The effects of molecular chaperones, protein aggregation and macromolecular crowding on protein folding have been studied.
研究了细胞内存在的分子伴侣、蛋白质聚集和大分子拥挤环境对蛋白质折叠的影响。
The structural basis of molecular recognition in proteins is the specific three dimensional structure or folding of the proteins, the information for which is contained in the sequence.
蛋白质分子识别的结构基础是蛋白质的三维结构或折叠，其信息存在于氨基酸序列中。
Recently studies on mechanism of oxidative protein folding and the role of molecular chaperones in protein quality control.
近年来深入研究蛋白质氧化折叠机制以及分子伴侣在蛋白质质量控制中的作用。
This paper summarizes some of the domestic research results in recent years, focus on the molecular dynamics simulations and simulated folding process.
本文总结了国内近几年的一些研究成果，重点讲述了分子动力学模拟和折叠过程的模拟。
Normal cells respond to ER stress by increasing transcription of genes encoding ER-resident molecular chaperones such as GRP94, GRP78 and PDI to facilitate protein folding.
细胞对这种应激的反应是增加一系列内质网分子伴侣如GRP94、GRP78和PDI等的表达。
There are two kinds of molecular chaperones playing critical roles in the folding of protein in E. coli.
蛋白的折叠大多需要分子伴侣的协助才能完成，其中有两类分子伴侣对蛋白的折叠有重要的影响。
There are two kinds of molecular chaperones playing critical roles in the folding of protein in E. coli.
蛋白的折叠大多需要分子伴侣的协助才能完成，其中有两类分子伴侣对蛋白的折叠有重要的影响。
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