Is the unfolded state the rosetta stone of the protein folding problem?
Is the unfolded state the rosetta stone of the protein folding problem?
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DOI：
10.1006/bbrc.2000.3360
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发表时间：
2000-09-24
影响因子：
3.1
通讯作者：
Carlsson, U
中科院分区：
文献类型：
--
作者：
Hammarström, P;Carlsson, U
解决蛋白质折叠问题是后基因组时代最具挑战性的任务之一。折叠起始位点的鉴定对于了解蛋白质折叠机制是非常重要的。检测未折叠蛋白的残馀结构可以提供蛋白质折叠起始位点的重要线索。大量研究的蛋白质在聚集在蛋白质核心的疏水区域中具有残余结构。这些稳定的结构可以作为折叠过程中的种子。此外，二级结构的局部偏好（β -sheet起始的旋转形式和cu-helix形成的螺旋形式）可以指导折叠反应。在这方面，在增加结构分辨率下研究的未折叠状态可以成为蛋白质折叠问题的罗塞塔石碑。(C) 2000年学术出版社。
Solving the protein folding problem is one of the most challenging tasks in the post genomic era. Identification of folding-initiation sites is very important in order to understand the protein folding mechanism. Detection of residual structure in unfolded proteins can yield important clues to the initiation sites in protein folding. A substantial number of studied proteins possess residual structure in hydrophobic regions clustered together in the protein core. These stable structures can work as seeds in the folding process. In addition, local preferences for secondary structure in the form of turns for beta-sheet initiation and helical turns for cu-helix formation can guide the folding reaction. In this respect the unfolded states, studied at increasing structural resolution, can be the Rosetta Stone of the protein folding problem. (C) 2000 Academic Press.