弹性蛋白
序列(生物学)
电磁线圈
过渡(遗传学)
生物物理学
结晶学
化学
材料科学
生物
生物化学
遗传学
工程类
基因
电气工程
作者
Tatiana I. Morozova,Nicolás García,Jean‐Louis Barrat
标识
DOI:10.1021/acs.jpclett.4c02568
摘要
It appeared certain that elastin condensates retain liquid-like properties. However, a recent experimental study demonstrated that their aggregate states might depend on the length of hydrophobic domains. To gain microscopic insight into this behavior, we employ atomistic modeling to assess the conformational properties of hydrophobic elastin-like polypeptides (ELPs). We find that short ELPs always remain in coil-like conformations, while the longer ones prefer globule states. While the former engages in intrapeptide hydrogen bonds temporarily, retaining their liquid-like properties, the latter forms hundreds of nanosecond-long intrapeptide hydrogen bonds attributed to ordered secondary structure motifs. Our work demonstrates that the sequence length modulates the material properties of elastin condensates.
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