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使用硬件加速在大型蛋白质序列集中检测单个α螺旋。

Detection of single alpha-helices in large protein sequence sets using hardware acceleration.

机构信息

Faculty of Information Technology and Bionics, Pázmány Péter Catholic University, Budapest, Hungary.

Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.

出版信息

J Struct Biol. 2018 Oct;204(1):109-116. doi: 10.1016/j.jsb.2018.06.005. Epub 2018 Jun 13.

DOI:10.1016/j.jsb.2018.06.005
PMID:29908248
Abstract

Single alpha-helices (SAHs) are increasingly recognized as important structural and functional elements of proteins. Comprehensive identification of SAH segments in large protein datasets was largely hindered by the slow speed of the most restrictive prediction tool for their identification, FT_CHARGE on common hardware. We have previously implemented an FPGA-based version of this tool allowing fast analysis of a large number of sequences. Using this implementation, we have set up of a semi-automated pipeline capable of analyzing full UniProt releases in reasonable time and compiling monthly updates of a comprehensive database of SAH segments. Releases of this database, denoted CSAHDB, is available on the CSAHserver 2 website at csahserver.itk.ppke.hu. An overview of human SAH-containing sequences combined with a literature survey suggests specific roles of SAH segments in proteins involved in RNA-based regulation processes as well as cytoskeletal proteins, a number of which is also linked to the development and function of synapses.

摘要

单 α-螺旋(SAHs)被越来越多地认为是蛋白质的重要结构和功能元件。全面识别大型蛋白质数据集的 S AH 片段,在很大程度上受到最具限制性的 S AH 预测工具的速度限制,该工具在通用硬件上进行识别时速度较慢。我们之前已经实现了该工具的基于 FPGA 的版本,允许快速分析大量序列。使用此实现,我们已经建立了一个半自动化管道,能够在合理的时间内分析完整的 UniProt 版本,并每月更新包含 S AH 片段的综合数据库。该数据库的版本称为 CSAHDB,可在 CSAHserver 2 网站 csahserver.itk.ppke.hu 上获得。对包含 S AH 的人类序列的概述结合文献调查表明,S AH 片段在涉及基于 RNA 的调节过程以及细胞骨架蛋白的蛋白质中具有特定作用,其中一些也与突触的发育和功能有关。

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Occurrence of Ordered and Disordered Structural Elements in Postsynaptic Proteins Supports Optimization for Interaction Diversity.
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Entropy (Basel). 2019 Aug 6;21(8):761. doi: 10.3390/e21080761.