PREDICTING CONFORMATIONAL SWITCHES IN PROTEINS

我们正在开发一种新的计算技术来预测 蛋白质中氨基酸的构象转换元素 序列。这种方法被称为ASP(矛盾结构预测器) 分析二级结构预测算法的结果以 确定构象矛盾的区域。ASP标识 测试蛋白质序列中具有功能的矛盾价区 涉及到大量的主干重新安排。以前的站点 被描述为构象开关被正确地预测为 结构矛盾地区的一部分。ASP还可以识别 核苷酸之间变构通讯的可能途径， 肌球蛋白的肌动蛋白结合和支点位置。该中心的设施 计算机图形学实验室用于获取序列数据和 二级结构预测。分子图形学是 数据分析，因为我们将结构性矛盾心理的预测映射到 蛋白质的三维晶体结构。我们的进一步发展 算法可以为指导实验研究提供一种工具 在缺乏详细信息的情况下蛋白质的功能和运动 三维结构数据。

We are developing a new computational technique to predict conformationally switching elements in proteins from their amino acid sequences. The method, called ASP (Ambivalent Structure Predictor) analyzes results from a secondary structure prediction algorithm to identify regions of conformational ambivalence. ASP identifies ambivalent regions in test protein sequences for which function involves substantial backbone rearrangements. Sites previously described as conformational switches are correctly predicted to be part of structurally ambivalent regions. ASP can also identify putative pathways of allosteric communication between the nucleotide, actin binding and fulcrum sites of myosin. The facilities at the Computer Graphics Laboratory are used to acquire sequence data and secondary structure predictions. Molecular graphics are integral to data analysis, as we map predictions of structural ambivalence onto the 3D crystal structures of the proteins. Further development of our algorithm may provide a tool for guiding experimental studies on protein function and motion in the absence of detailed three-dimensional structural data.