A new way to recognize downhill folding based on generalized path length

IF 2.4 Q3 Computer Science
Xuewei Jiang, Zhengwu Wu, Z. Fan, Junhua Yin, Lu Zheng
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引用次数: 1

Abstract

The protein folding is an important scientific problem and many methods were designed to elucidate the protein folding and obtain insight into the molecular mechanism. A novel means is presented to identify the downhill pathways of protein folding in this paper. This method is based on barrier energy profile projected onto the generalized path length (GPL) with Breadth-first searching (BFS) algorithm. We show the effectiveness of this approach by constructing the barrier energy profile of trpzip2 and comparing with other methods.
基于广义路径长度的下坡折叠识别新方法
蛋白质折叠是一个重要的科学问题,人们设计了许多方法来阐明蛋白质折叠并深入了解其分子机制。本文提出了一种新的方法来识别蛋白质折叠的下行途径。该方法基于广义路径长度(GPL)上的势垒能量分布,采用广度优先搜索(BFS)算法。我们通过构建trpzip2的势垒能量分布并与其他方法进行比较,证明了该方法的有效性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
CiteScore
1.70
自引率
0.00%
发文量
0
审稿时长
3 months
期刊介绍: The Journal of Theoretical and Computational Chemistry (JTCC) is an international interdisciplinary journal aimed at providing comprehensive coverage on the latest developments and applications of research in the ever-expanding field of theoretical and computational chemistry. JTCC publishes regular articles and reviews on new methodology, software, web server and database developments. The applications of existing theoretical and computational methods which produce significant new insights into important problems are also welcomed. Papers reporting joint computational and experimental investigations are encouraged. The journal will not consider manuscripts reporting straightforward calculations of the properties of molecules with existing software packages without addressing a significant scientific problem. Areas covered by the journal include molecular dynamics, computer-aided molecular design, modeling effects of mutation on stability and dynamics of macromolecules, quantum mechanics, statistical mechanics and other related topics.
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