Conformation-dependent design of protein-like copolymers: Molecular-dynamic modelingстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
Местоположение издательства:Road Town, United Kingdom
Первая страница:66
Последняя страница:73
Аннотация:A transition from random copolymerization to conformation-dependent design is found to be controlled by the following conditions: the threshold degree of polymerization of a macroradical, the copolymer composition, and the reaction rate. In the case of copolymerization accompanied by conformation-dependent design, copolymers form a protein-like globule that is composed of a hydrophobic core and a polar shell. As hydrophobic monomers are selectively sorbed by the globule core, their involvement in polymerization is preferential. Primary sequences of copolymers are not uniform due to a change in the copolymerization regime with increasing the macroradical length. The size distribution of blocks in primary sequences is described by a power law. The reason behind this behavior is likely related to a close connection between the position of the active site relative to the globule-solution boundary and the type of monomers that are preferentially added during polymerization.