Capturing Nested Information from Disordered Peptide Phases
Capturing Nested Information from Disordered Peptide Phases
复制标题
从无序肽相中捕获嵌套信息
DOI：
10.1002/pep2.24215
复制
发表时间：
2021
期刊：
影响因子：
2.4
通讯作者：
Lynn, David G
中科院分区：
文献类型：
--
作者：
Gordon, Christella K;Luu, Regina;Lynn, David G
安芬森的教条源于实验，实验表明蛋白质的天然 3D 折叠结构是在其一级序列中编码的。这一见解是在近 40% 的真核蛋白被发现含有本质上无序的结构域以及能够模板化多种结构和功能输出的结合配偶体之前出现的。尽管表征这种本质上无序的蛋白质结构域及其与各种结合伙伴的相互作用存在挑战，但了解它们如何传播和调节上下文相关信息的需要现在变得越来越重要。除了了解多细胞生物的复杂信号网络之外，利用它们的潜力还将扩展下一代功能材料。因此，我们回顾了模型肽的进展，以揭示多肽材料精确时空组装所需的规则。
Anfinsen's dogma emerged from experiments which show that a protein's native 3D folded architecture is encoded within its primary sequence. This insight emerged before almost 40% of eukaryotic proteins were found to contain intrinsically disordered domains with binding partners that are able to template multiple structures and functional outputs. Despite the challenges associated with characterizing such intrinsically disordered protein domains and their interactions with various binding partners, the need to understand how they propagate and regulate context‐dependent information now becomes increasingly important. In addition to understanding the complex signaling networks of multicellular organisms, harness their potential will expand the next generation of functional materials. Accordingly, we review progress with model peptides to reveal the rules necessary for precise spatiotemporal assembly of polypeptide materials.