Structural changes of a protein bound to a polyelectrolyte depend on the hydrophobicity and polymerization degree of the polyelectrolyteстатья
Информация о цитировании статьи получена из
Web of Science ,
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Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
Авторы:
Stogov S.V.a ,
Izumrudov V.A.b ,
Muronetz V.I.a.c
Журнал:
Biochemistry (Moscow)
Том:
75
Номер:
4
Год издания:
2010
Издательство:
Pleiades Publishing, Ltd
Местоположение издательства:
Road Town, United Kingdom
Первая страница:
437
Последняя страница:
442
DOI:
10.1134/S0006297910040061
Аннотация:
Influence of polyelectrolytes of different chemical structure and degree of polymerization on aggregation and denaturation of the oligomeric enzyme glyceraldehyde-3-phosphate dehydrogenase has been studied to ascertain molecu- lar characteristics of the polymer chains providing the efficient prevention of aggregation of the enzyme without drastic changes in its structure and catalytic activity. The best polymers meeting these requirements were found to be hydrophilic high-molecular-weight polyelectrolytes forming stable complexes with the enzyme. The revealed pronounced negative effect of short polymer chains on the enzyme must be taken into account in the design of protein-polyelectrolyte systems by using thoroughly fractionated polymer samples containing no admixture of charged oligomers. © Pleiades Publishing, Ltd., 2010.
Добавил в систему:
Изумрудов Владимир Алексеевич