Phillips J C
Department of Physics and Astronomy, Rutgers University, Piscataway, NJ 08854, USA.
Proc Natl Acad Sci U S A. 2009 Mar 3;106(9):3107-12. doi: 10.1073/pnas.0811262106. Epub 2009 Feb 13.
The complexity of proteins is substantially simplified by regarding them as archetypical examples of self-organized criticality (SOC). To test this idea and elaborate on it, this article applies the Moret-Zebende SOC hydrophobicity scale to the large-scale scaffold repeat protein of the HEAT superfamily, PR65/A. Hydrophobic plasticity is defined and used to identify docking platforms and hinges from repeat sequences alone. The difference between the MZ scale and conventional hydrophobicity scales reflects long-range conformational forces that are central to protein functionality.
将蛋白质视为自组织临界性（SOC）的典型例子，可大大简化其复杂性。为了验证并详细阐述这一观点，本文将莫雷特 - 泽本德（Moret-Zebende）SOC疏水性标度应用于HEAT超家族的大规模支架重复蛋白PR65/A。定义了疏水性可塑性，并仅从重复序列中识别对接平台和铰链。MZ标度与传统疏水性标度之间的差异反映了对蛋白质功能至关重要的长程构象力。
