蛋白质的自组织临界性：G蛋白偶联受体的亲水粗糙化
Self-Organized Criticality in Proteins: Hydropathic Roughening Profiles of G-Protein Coupled Receptors
摘要：
蛋白质似乎是自组织临界性（SOC）最引人注目的自然例子，SOC这个概念解释了许多其他显然不可能的现象。蛋白质构象功能通常由长程疏水（疏/亲）相互作用主导，其既驱动蛋白质压缩又介导蛋白质-蛋白质相互作用。超家族跨膜GPCR是人类基因组中最大的蛋白质家族;它们的氨基酸序列形成了蛋白质-膜相互作用的最大数据库。虽然现在有几个heptad家族的代表的heptad跨膜结构的结构数据，在这里，我们表明，新的见解全球和一些地方的化学趋势GPCR性能可以准确地从单独的序列，特别是通过分离的细胞外和细胞质环跨膜段。长程水-蛋白质相互作用的全局介导与粗糙界面对这些相互作用的调制一起发生。这里仅根据氨基酸序列定义了亲水粗糙化特征，并且不需要蛋白质坐标的知识。GPCR和一些更简单的蛋白质家族的粗糙化概况显示与蛋白质功能的准确和透明的连接。
英文摘要：
Proteins appear to be the most dramatic natural example of self-organized criticality (SOC), a concept that explains many otherwise apparently unlikely phenomena. Protein conformational functionality is often dominated by long-range hydro(phobic/philic) interactions which both drive protein compaction and mediate protein-protein interactions. Superfamily transmembrane GPCR are the largest family of proteins in the human genome; their amino acid sequences form the largest data base for protein-membrane interactions. While there are now structural data on the heptad transmembrane structures of representatives of several heptad families, here we show that fresh insights into global and some local chemical trends in GPCR properties can be obtained accurately from sequences alone, especially by separating the extracellular and cytoplasmic loops from transmembrane segments. The global mediation of long-range water-protein interactions occurs in conjunction with modulation of these interactions by roughened interfaces. Hydropathic roughening profiles are defined here solely in terms of amino acid sequences, and knowledge of protein coordinates is not required. Roughening profiles both for GPCR and some simpler protein families display accurate and transparent connections to protein functionality.
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