蛋白质三级结构中α-螺旋主链修饰的设计策略比较。
Comparison of design strategies for α-helix backbone modification in a protein tertiary fold.
作者信息
Tavenor Nathan A, Reinert Zachary E, Lengyel George A, Griffith Brian D, Horne W Seth
机构信息
Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA.
出版信息
Chem Commun (Camb). 2016 Mar 7;52(19):3789-92. doi: 10.1039/c6cc00273k.
Abstract
We report here the comparison of five classes of unnatural amino acid building blocks for their ability to be accommodated into an α-helix in a protein tertiary fold context. High-resolution structural characterization and analysis of folding thermodynamics yield new insights into the relationship between backbone composition and folding energetics in α-helix mimetics and suggest refined design rules for engineering the backbones of natural sequences.
摘要
我们在此报告了五类非天然氨基酸构建模块在蛋白质三级折叠环境中被纳入α-螺旋的能力的比较。高分辨率结构表征和折叠热力学分析为α-螺旋模拟物中主链组成与折叠能量学之间的关系提供了新见解，并为设计天然序列的主链提出了改进的设计规则。
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