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Changes in the thermal unfolding of p-phenylenedimaleimide-modified myosin subfragment 1 induced by its ’weak’ binding to F-actinстатья
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: 18 июля 2013 г.
- Авторы: Kaspieva O.V., Nikolaeva O.P., Orlov V.N., Ponomarev M.A., Drachev V.A., Levitsky D.I.
- Журнал: FEBS Letters
- Том: 489
- Номер: 2-3
- Год издания: 2001
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 144
- Последняя страница: 148
- Аннотация: Differential scanning calorimetry (DSC) was used to analyze the thermal unfolding of myosin subfragment 1 (S1) with the SH1 (Cys-707) and SH2 (Cys-697) groups cross-linked by N,N’-p-phenylenedimaleimide (pPDM-S1). It has been shown that F-actin affects the thermal unfolding of pPDM-S1 only at very low ionic strength, when some part of pPDM-S1 binds weakly to F-actin, but not at higher ionic strength (200 mM KCl). The weak binding of pPDM-S1 to F-actin shifted the thermal transition of pPDM-S1 by about 5 degrees C to a higher temperature. This actin-induced increase in thermal stability of pPDM-S1 was similar to that observed with ’strong’ binding of unmodified S1 to F-actin. Our results show that actin-induced structural changes revealed by DSC in the myosin head occur not only upon strong binding but also on weak binding of the head to F-actin, thus suggesting that these changes may occur before the power-stroke and play an important role in the motor function of the head.
- Добавил в систему: Орлов Виктор Николаевич