摘要翻译：
本文回顾了蛋白质标度理论的发展，从数学和统计力学的背景出发，并引向生物医学的应用。进化以不同的方式组织了每个蛋白质家族，但标度理论既简单又有效，为在线蛋白质数据库(PDB)中包含的9万个静态结构中的许多蛋白质提供了易于转移的动力学见解。标度理论是一个简化的魔杖，它使人们能够搜索科学网中数以亿计的蛋白质文章，并识别那些通过单个蛋白质序列为疾病的早期检测和/或治疗提供新的成本效益方法的蛋白质（个性化医学）。临界点理论是通用的，最近它被证明是描述蛋白质网络的最有效的方法，这些网络在给定的环境中已经进化到接近完美的功能（自组织临界性）。进化模式由共同的标度原则控制，可以使用通过研究数千个PDB结构而开发的生物信息学标度来量化这些标度。最有效的尺度包括以膜尺寸为中心的长度尺度上平均的水病理球形雕塑相互作用，或与聚集（强）蛋白-蛋白相互作用相关的暴露β链倾向。
---
英文标题：
《Quantitative Molecular Scaling Theory of Protein Amino Acid Sequences,
  Structure, and Functionality》
---
作者：
J. C. Phillips
---
最新提交年份：
2016
---
分类信息：

一级分类：Quantitative Biology        数量生物学
二级分类：Other Quantitative Biology        其他定量生物学
分类描述：Work in quantitative biology that does not fit into the other q-bio classifications
不适合其他q-bio分类的定量生物学工作
--

---
英文摘要：
  Here we review the development of protein scaling theory, starting from backgrounds in mathematics and statistical mechanics, and leading to biomedical applications. Evolution has organized each protein family in different ways, but scaling theory is both simple and effective in providing readily transferable dynamical insights complementary for many proteins represented in the 90 thousand static structures contained in the online Protein Data Base (PDB). Scaling theory is a simplifying magic wand that enables one to search the hundreds of millions of protein articles in the Web of Science, and identify those proteins that present new cost-effective methods for early detection and/or treatment of disease through individual protein sequences (personalized medicine). Critical point theory is general, and recently it has proved to be the most effective way of describing protein networks that have evolved towards nearly perfect functionality in given environments (self-organized criticality). Evolutionary patterns are governed by common scaling principles, which can be quantified using scales that have been developed bioinformatically by studying thousands of PDB structures. The most effective scales involve either hydropathic globular sculpting interactions averaged over length scales centered on membrane dimensions, or exposed beta strand propensities associated with aggregative (strong) protein-protein interactions.
---
PDF链接：
https://arxiv.org/pdf/1610.04116