 | Название: | NMR Studies of Structural Motifs: Protein Folding and Ligand Binding |
| Автор: | Christine Sallum | |
| Год: | 2010 | |
| ISBN: | 3838335775 | |
| Количество страниц: | 176 | |
| Цена: | 9 975 руб. | |
| Описание: | NMR of Structural Motifs: The agrin G3 domain is critical in development and maintenance of the neuromuscular junction. G3 binds -dystroglycan and initiates acetylcholine receptor clustering on myotube membranes. Using NMR spectroscopy, we show both active B8 and inactive B0 isoforms binding sialic acid, heparin, and heparan sulfate and map the binding sites. Ligand dissociation constants were determined by isothermal titration calorimetry. Pulse field gradient diffusion NMR was used to determine heparin binding stoichiometry, 2 protein per heparin. Residual dipolar couplings (RDCs) were used to probe residual denatured OB-fold protein structure; folded staphylococcal nuclease (SN) has greater RDC differences. Invariance of denatured SN RDCs had been attributed to robustness of long-range denatured state structure. We show, however, that increased RDC differences in the folded states are a consequence of close packing of native state polypeptide, more consistent with... |
Структура:
Списки:
Сложность материала:
Величины и единицы:
Книги Список книг
Новейшие методы исследования биосистем Книга охватывает широкий круг методов, таких как молекулярная динамика, ...
Введение в молекулярную биологию Книга представляет собой переработанный курс лекций, который авторы читают ...
Asphaltenes: Chemical Transformation during Hydroprocessing of Heavy Oils (Chemical Industries) During the upgrading of heavy petroleum, asphaltene is the most problematic impurity since it is the main cause of catalyst deactivation and sediments ...
Химия билирубина и его аналогов В настоящей монографии изложены результаты фундаментальных и прикладных ...