Guelph-Waterloo Centre for Graduate Work in Chemistry and Biochemistry, Department of Chemistry, University of Waterloo, 200 University Avenue, Waterloo, Ontario, Canada.
Protein Eng Des Sel. 2011 Jan;24(1-2):213-7. doi: 10.1093/protein/gzq099. Epub 2010 Nov 17.
The energetic networks that govern regulated switching processes in macromolecules are poorly understood at a molecular level. We illustrate a general methodology that uses thermodynamic cycles to measure the coupling energetics between specific groups in a macromolecule and ligand-binding-induced macromolecular switching. The approach is applied to new and published thermodynamic stability and/or binding data not previously analyzed in this way, for a wide range of switching systems, including H+ or Ca²+-binding-induced myristoyl switching, ion or peptide-binding-induced conformational switching in various proteins and small molecule binding to a ribo-switch. The results show how this powerful approach can be used to identify and dissect the molecular determinants of switching in macromolecules.
在分子水平上，调控大分子中开关过程的能量网络的理解还很不完善。我们展示了一种通用方法，该方法使用热力学循环来测量大分子中特定基团与配体结合诱导的大分子开关之间的耦合能。该方法应用于新的和已发表的热力学稳定性和/或结合数据，这些数据以前没有以这种方式进行分析，涵盖了广泛的开关系统，包括 H+或 Ca²+结合诱导的豆蔻酰开关、各种蛋白质中离子或肽结合诱导的构象开关以及小分子与核酶的结合。结果表明，这种强大的方法如何用于识别和剖析大分子开关的分子决定因素。
