Sarakatsannis James N, Duan Yong
Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware, USA.
Proteins. 2005 Sep 1;60(4):732-9. doi: 10.1002/prot.20549.
The structure and folding mechanism of a given protein are determined by many factors, including the electrostatic interactions between charged residues of protein molecules known in general as salt bridges. In this study, analyses were conducted on 10,370 salt bridges in 2017 proteins and the results compared to previous statistical surveys of 36 protein structures. Although many of the general trends remained consistent with other studies, more detailed information was illuminated by the larger dataset. In particular, it was shown that there is a strong correlation between secondary structure and salt bridge formation, and that salt bridges display preferential formation in an environment of about 30% solvent accessible surface area.
给定蛋白质的结构和折叠机制由许多因素决定，包括蛋白质分子带电残基之间的静电相互作用，一般称为盐桥。在本研究中，对2017种蛋白质中的10370个盐桥进行了分析，并将结果与之前对36种蛋白质结构的统计调查进行了比较。尽管许多总体趋势与其他研究一致，但更大的数据集揭示了更详细的信息。特别是，研究表明二级结构与盐桥形成之间存在很强的相关性，并且盐桥在约30%溶剂可及表面积的环境中表现出优先形成。
