文章基本信息

标题：Altering dimerization specificity by changes in surface electrostatics
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作者：M. J. Nohaile ; Z. S. Hendsch ; B. Tidor 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2001
卷号：98
期号：6
页码：3109-3114
DOI：10.1073/pnas.051624498
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Arc repressor forms a homodimer in which the subunits intertwine to create a single globular domain. To obtain Arc sequences that fold preferentially as heterodimers, variants with surface patches of excess positive or negative charge were designed. Several but not all oppositely charged sequence pairs showed preferential heterodimer formation. In the most successful design pair, helix B of one subunit contained glutamic acids at positions 43, 46, 47, 48, and 50, whereas the other subunit contained lysines or arginines at these positions. A continuum electrostatic model captures many features of the experimental results and suggests that the most successful designs include elements of both positive and negative design.
关键词：Arc repressor ; continuum electrostatics ; heterodimer ; negative design ; protein stability