School of Biological Sciences, Indian Institute of Technology Delhi, New Delhi, India.
J Biomol Struct Dyn. 2011 Feb;28(4):443-54. doi: 10.1080/073911011010524954.
Folding of naturally occurring proteins has eluded a universal molecular level explanation till date. Rather, there is an abundance of diverse views on dominant factors governing protein folding. Through rigorous analyses of several thousand crystal structures, we observe that backbones of folded proteins display some remarkable invariant features. Folded proteins are characterized by spatially well-defined, distance dependent, and universal, neighborhoods of amino acids which defy any of the conventionally prevalent views. These findings present a compelling case for a newer view of protein folding which takes into account solvent mediated and amino acid shape and size assisted optimization of the tertiary structure of the polypeptide chain to make a functional protein.
到目前为止，天然蛋白质的折叠仍然无法用普遍的分子水平解释。相反，对于主导蛋白质折叠的因素存在着大量不同的观点。通过对数千个晶体结构的严格分析，我们观察到折叠蛋白质的骨架表现出一些显著的不变特征。折叠蛋白质的特点是空间上定义明确、距离依赖和普遍的氨基酸邻域，这与传统上流行的观点都不相符。这些发现为一种新的蛋白质折叠观点提供了强有力的证据，该观点考虑了溶剂介导的和氨基酸形状和大小辅助的多肽链三级结构的优化，以形成功能性蛋白质。
