Molecular Structure and Function, Hospital for Sick Children, Toronto, Canada.
Adv Exp Med Biol. 2012;725:159-83. doi: 10.1007/978-1-4614-0659-4_10.
An emerging class of disordered proteins underlies the elasticity of many biological tissues. Elastomeric proteins are essential to the function of biological machinery as diverse as the human arterial wall, the capture spiral of spider webs and the jumping mechanism of fleas. In this chapter, we review what is known about the molecular basis and the functional role of structural disorder in protein elasticity. In general, the elastic recoil of proteins is due to a combination of internal energy and entropy. In rubber-like elastomeric proteins, the dominant driving force is the increased entropy of the relaxed state relative to the stretched state. Aggregates of these proteins are intrinsically disordered or fuzzy, with high polypeptide chain entropy. We focus our discussion on the sequence, structure and function of five rubber-like elastomeric proteins, elastin, resilin, spider silk, abductin and ColP. Although we group these disordered elastomers together into one class of proteins, they exhibit a broad range of sequence motifs, mechanical properties and biological functions. Understanding how sequence modulates both disorder and elasticity will help advance the rational design of elastic biomaterials such as artificial skin and vascular grafts.
一类新兴的无序蛋白是许多生物组织弹性的基础。弹性蛋白是多种生物机制（如人类动脉壁、蜘蛛蛛网的捕捉螺旋和跳蚤的跳跃机制）正常运转所必需的。在本章中，我们综述了关于结构无序在蛋白弹性中的分子基础和功能作用的已有认识。一般来说，蛋白的弹性回缩是由内能和熵共同作用的结果。在类似橡胶的弹性蛋白中，主要驱动力是松弛态相对于拉伸态的熵增加。这些蛋白的聚集体本质上是无序的或模糊的，具有高分子链熵。我们的讨论集中在 5 种类似橡胶的弹性蛋白（弹性蛋白、松弛素、蜘蛛丝、abductin 和 ColP）的序列、结构和功能上。尽管我们将这些无序弹性蛋白归为一类，但它们表现出广泛的序列基序、力学性能和生物学功能。了解序列如何调节无序和弹性，将有助于推进弹性生物材料（如人工皮肤和血管移植物）的合理设计。
