Probing the spectral signatures of orange carotenoid protein by orthogonal translation with aromatic non-canonical amino acids

Hsueh-Wei, T.; Moldenhauer, M.; Friedrich, T.; Maksimov, E.G.; Budisa, N.

Информация о цитировании статьи получена из Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 1 июня 2022 г.

Авторы: Hsueh-Wei Tseng, Moldenhauer Marcus, Friedrich Thomas, Maksimov Eugene G., Budisa Nediljko
Журнал: Biochemical and Biophysical Research Communications
Том: 607
Год издания: 2022
Издательство: Academic Press
Местоположение издательства: United States
Первая страница: 96
Последняя страница: 102
DOI: 10.1016/j.bbrc.2022.03.118
Аннотация: Orange Carotenoid Protein (OCP) is a water-soluble photoreceptor involved in photoprotection of cyanobacteria. The photoactive OCP contains a bound ketocarotenoid cofactor held in a protein matrix with a hydrogen bonding network. We have developed a system to replace essential residues of the photoactive OCP with non-canonical aromatic analogues that produce well-defined chemical or steric changes. Preliminary spectroscopic evaluation of the generated OCP variants demonstrates the potential of this "molecular surgery" to disentangle protein-chromophore interaction networks that are critical for photoreceptor function. In this way, the number and strength of key contacts with non-canonical amino acids could be controlled and manipulated. We have illustrated this principle here by replacing hydrogen bond donating residues with aromatic non-canonical amino acids that alter the state preference of OCP.
Добавил в систему: Максимов Евгений Георгиевич

	ИСТИНА	Войти в систему Регистрация
	ФНКЦ РР
	Главная Поиск Статистика О проекте Помощь

ИСТИНА

ФНКЦ РР

Probing the spectral signatures of orange carotenoid protein by orthogonal translation with aromatic non-canonical amino acidsстатья

Прикрепленные файлы