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Protein Interaction with Charged Macromolecules: From Model Polymers to Unfolded Proteins and Post-Translational Modificationsстатья
Статья опубликована в высокорейтинговом журнале
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: 11 апреля 2019 г.
- Авторы: Semenyuk Pavel, Muronetz Vladimir
- Журнал: International Journal of Molecular Sciences
- Том: 20
- Номер: 5
- Год издания: 2019
- Издательство: MDPI
- Местоположение издательства: Basel, Switzerland
- Первая страница: 1252
- DOI: 10.3390/ijms20051252
- Аннотация: Interaction of proteins with charged macromolecules is involved in many processes in cells. Firstly, there are many naturally occurred charged polymers such as DNA and RNA, polyphosphates, sulfated glycosaminoglycans, etc., as well as pronouncedly charged proteins such as histones or actin. Electrostatic interactions are also important for “generic” proteins, which are not generally considered as polyanions or polycations. Finally, protein behavior can be altered due to post-translational modifications such as phosphorylation, sulfation, and glycation, which change a local charge of the protein region. Herein we review molecular modeling for the investigation of such interactions, from model polyanions and polycations to unfolded proteins. We will show that electrostatic interactions are ubiquitous, and molecular dynamics simulations provide an outstanding opportunity to look inside binding and reveal the contribution of electrostatic interactions. Since a molecular dynamics simulation is only a model, we will comprehensively consider its relationship with the experimental data.
- Добавил в систему: Семенюк Павел Игоревич