Suppr超能文献

一种与λ-N蛋白的基序肽特异性相互作用的新型稳定RNA五聚体环。

A novel stable RNA pentaloop that interacts specifically with a motif peptide of lambda-N protein.

作者信息

Kawakami Junji, Sugimoto Naoki, Tokitoh Hisanori, Tanabe Yoshiatsu

机构信息

Frontier Institute for Biomolecular Engineering Research (FIBER), Konan University, Higashinada-ku, Kobe, Japan.

出版信息

Nucleosides Nucleotides Nucleic Acids. 2006;25(4-6):397-416. doi: 10.1080/15257770600684027.

Abstract

To achieve a novel specific peptide-nucleic acid binding model, we designed an in vitro selection procedure to decrease the energetic contribution of the electrostatic interaction in the total binding energy and to increase the contribution of hydrogen bonding and pi-pi stacking. After the selection of hairpin-loop RNAs that specifically bound to a model peptide of lambda N protein (N peptide), a new thermostable pentaloop RNA motif (N binding thermostable RNA hairpin: NTS RNA) was revealed. The obtained NTS RNA was able to bind to the N peptide with superior specificity to the boxB RNA, which is the naturally occurring partner of the lambda N protein.

摘要

为了实现一种新型的特异性肽 - 核酸结合模型,我们设计了一种体外筛选程序,以降低静电相互作用在总结合能中的能量贡献,并增加氢键和π-π堆积的贡献。在筛选出与λN蛋白的模型肽(N肽)特异性结合的发夹环RNA后,揭示了一种新的热稳定五碱基环RNA基序(N结合热稳定RNA发夹:NTS RNA)。所获得的NTS RNA能够以比boxB RNA更高的特异性与N肽结合,boxB RNA是λN蛋白的天然结合伴侣。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验