三螺旋
赖氨酸
背景(考古学)
超分子化学
共价键
化学
螺旋(腹足类)
胶原螺旋
电荷(物理)
立体化学
结晶学
氨基酸
生物物理学
生物化学
物理
晶体结构
生物
有机化学
古生物学
生态学
量子力学
蜗牛
作者
Carson C. Cole,Le Tracy Yu,Mikita Misiura,Joseph W. Williams,Tien D. Bui,Jeffrey D. Hartgerink
标识
DOI:10.1021/acs.biomac.3c00680
摘要
Collagen mimetic peptides are composed of triple helices. Triple helical formation frequently utilizes charge pair interactions to direct protein assembly. The design of synthetic triple helices is challenging due to the large number of competing species and the overall fragile nature of collagen mimetics. A successfully designed triple helix incorporates both positive and negative criteria to achieve maximum specificity of the supramolecular assembly. Intrahelical charge pair interactions, particularly those involved in lysine–aspartate and lysine–glutamate pairs, have been especially successful both in driving helix specificity and for subsequent stabilization by covalent capture. Despite this progress, the important sequential and geometric relationships of charged residues in a triple helical context have not been fully explored for either supramolecular assembly or covalent capture stabilization. In this study, we compare the eight canonical axial and lateral charge pairs of lysine and arginine with glutamate and aspartate to their noncanonical, reversed charge pairs. These findings are put into the context of collagen triple helical design and synthesis.
科研通智能强力驱动
Strongly Powered by AbleSci AI