论文标题
部分可观测时空混沌系统的无模型预测
Rethinking the protein folding problem from a new perspective
论文作者
论文摘要
阿芬森的主要关注点之一是揭示氨基酸序列与其生物活性构象之间的联系。这种搜索引起了结构生物学的两个关键问题，即蛋白质为什么折叠以及序列如何编码其折叠。关于原因，他提出了一个合理的答案，即，在给定的环境中，蛋白质将蛋白质折叠成其功能形式 - 天然状态 - 因为这种结构代表了所有可行的构象中最低的自由能最小值 - 热力学假设或anfinsen教条。至于方式，这仍然是一个未解决的挑战，因此，从新的角度研究了蛋白质折叠的新角度，即作为一个分析整体 - 莱布尼茨和康德提出的概念。这种新的观点迫使我们详细讨论为什么基于理论的力场方法的方法既无法准确预测蛋白质的三维结构，又以其能力回答结构生物学中最关键的问题之一：序列如何编码其折叠。
One of the main concerns of Anfinsen was to reveal the connection between the amino acid sequence and their biologically active conformation. This search gave rise to two crucial questions in structural biology, namely, why the proteins fold and how a sequence encodes its folding. As to the why, he proposes a plausible answer, namely, at a given milieu a protein folds into its functional form -- native state -- because such structure represents the lowest free-energy minimum among all feasible conformations -- the thermodynamic hypothesis or Anfinsen dogma. As to the how, this remains as an unsolved challenge and, hence, this inquiry is examined here from a new perspective of protein folding, namely, as an analytic whole -- a notion proposed by Leibnitz and Kant. This new perspective forces us to discuss in detail why the theoretical force-field-based approaches have failed in both their ability to predict the three-dimensional structure of a protein accurately and in their capacity to answer one of the most critical questions in structural biology: how a sequence encodes its folding.
