期刊
BIOCHEMISTRY-MOSCOW
卷 75, 期 7, 页码 912-918出版社
MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1134/S000629791007014X
关键词
cation-pi; secondary structure; long-range interactions; accessible surface area; stabilization centers; immunoglobulin proteins; structural stability
Cation-pi interactions are known to be important contributors to protein stability and ligand-protein interactions. In this study, we have analyzed the influence of cation-pi interactions in single chain immunoglobulin proteins. We observed 87 cation-pi interactions in a data set of 33 proteins. These interactions are mainly formed by long-range contacts, and there is preference of Arg over Lys in these interactions. Arg-Tyr interactions are predominant among the various pairs analyzed. Despite the scarcity of interactions involving Trp, the average energy for Trp-cation interactions is quite high. This information suggests that the cation-pi interactions involving Trp might be of high relevance to the proteins. Secondary structure analysis reveals that cation-pi interactions are formed preferably between residues in which at least one is in beta-strand. Proteins having beta-strand regions have the highest number of cation-pi interaction-forming residues.
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