Mannige Ranjan V
Molecular Foundry, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720,USA.
Proteomes. 2014 Mar 25;2(2):154-168. doi: 10.3390/proteomes2020154.
While the repertoire of protein folds that exists today underlies most of life's capabilities, our mechanistic picture of protein fold origination is incomplete. This paper discusses a hypothetical mechanism for the emergence of the protein fold repertoire from highly dynamic and collapsed peptides, exemplified by peptides with high oil content or hydrophobicity. These peptides are called pluripotent to emphasize their capacity to evolve into numerous folds transiently available to them. As evidence, the paper will discuss previous simulation work on the superior fold evolvability of oily peptides, trace ("fossil") evidence within proteomes seen today, and a general relationship between protein dynamism and evolvability. Aside from implications on the origination of protein folds, the hypothesis implies that the vanishing utility of a random peptide in protein origination may be relatively exaggerated, as some random peptides with a certain composition (e.g., oily) may fare better than others. In later sections, the hypothesis is discussed in the context of existing discussions regarding the spontaneous origination of biomolecules.
虽然如今存在的蛋白质折叠库构成了生命大多数功能的基础，但我们对蛋白质折叠起源的机制认识并不完整。本文讨论了一种从高度动态且折叠的肽段中产生蛋白质折叠库的假设机制，以高油含量或高疏水性的肽段为例。这些肽段被称为多能的，以强调它们能够演变成多种对其而言短暂可用的折叠形式的能力。作为证据，本文将讨论先前关于油性肽段卓越折叠可进化性的模拟研究、当今蛋白质组中可见的微量（“化石”）证据，以及蛋白质动态性与可进化性之间的一般关系。除了对蛋白质折叠起源的影响外，该假设还意味着在蛋白质起源中随机肽段无用性的消失可能被相对夸大了，因为某些具有特定组成（如油性）的随机肽段可能比其他肽段表现更好。在后续章节中，将在关于生物分子自发起源的现有讨论背景下对该假设进行探讨。
