Факторы, влияющие на скорость и эффективность котрансляционного сворачивания белка
Диссертация
Подходы к исследованию сворачивания белка разнообразны и многочисленны. Однако подавляющее большинство этих исследований относится к сворачиванию полноразмерных полипептидных цепей в нативную структуру, когда в качестве исходного состояния цепи выступает полностью или частично денатурированный белок. К настоящему времени установлено, что сворачивание белков в клетке происходит котрансляционно… Читать ещё >
Содержание
- ОБЗОР ЛИТЕРАТУРЫ
- Глава I. КОТРАНСЛЯЦИОННОЕ СВОРАЧИВАНИЕ БЕЛКОВ
- 1. 1. Гипотеза котрансляционного сворачивания белка
- 1. 2. Скорость и эффективность котрансляционного формирования дисульфидных связей
- 1. 3. Скорость и эффективность котрансляционного формирования нативной структуры
- 1. 4. Котрансляционная олигомеризация белков
- Глава II. ФАКТОРЫ КОТРАНСЛЯЦИОННОГО СВОРАЧИВАНИЯ БЕЛКА
- 2. 1. Вклад векторности синтеза белка на рибосоме в его котрансляционное сворачивание
- 2. 2. Влияние скорости синтеза белка на его котрансляционное сворачивание
- 2. 3. Вклад фиксации С конца растущего полипептида на рибосоме в его котрансляционное сворачивание
- 2. 4. Влияние рибосомного окружения растущей полипептидной цепи на её котрансляционное сворачивание
- 2. 4. 1. Стартовая конформациярастущего полипептида, задаваемая в пептидил-трансферазном центре рибосомы
- 2. 4. 2. Путь растущей цепи от пептидил-трансферазного центра к выходу из рибосомы
- 2. 4. 3. Сворачивание растущей полипептидной цепи внутри рибосомы
- 2. 5. Вклад молекулярных шаперонов в котрансляционное сворачивание белка
- 2. 5. 1. Молекулярные шапероны семейства Hsp
- 2. 5. 2. Молекулярные шапероны семейства Hsp
- 3. 1. Свойства фермента
- 3. 2. Люцифераза как объект исследований сворачивания белков
- 2. 1. Активность шаперонов Hsp70 в бактериальной бесклеточной системе трансляции
- 2. 2. Эффективность котрансляционного сворачивания люциферазы в присутствии шаперонов Hsp
- 2. 3. Длительность пост-трансляционного сворачивания люциферазы, синтезируемой в присутствии шаперонов Hsp
- 2. 4. Длительность пост-трансляционного сворачивания люциферазы, синтезируемой в присутствии триггер фактора
- 3. 1. Сворачивание полипептидной цепи люциферазы, иммобилизованной на гранулах сефарозы
- 3. 1. 1. Иммобилизация С конца люциферазы на гранулах хелирующей сефарозы
- 3. 1. 2. Сворачивание полипептидной цепи люциферазы на гранулах сефарозы
- 3. 1. 3. Зависимость эффективностиренатурации люциферазы от концентрации белка
- 3. 1. 4. Ренатурация иммобилизованной люциферазы при разной ионной силе
- 3. 2. Ренатурация люциферазы, иммобилизованной на рибосоме в виде пептидил-тРНК
- 3. 2. 1. Иммобилизация С конца люциферазы на 70S рибосоме
- 3. 2. 2. Ренатурация люциферазы, иммобилизованной на
- 70. S рибосоме
- 3. 2. 3. Влияние триггер фактора наренатурацию связанной с рибосомой люциферазы
- 4. 1. Влияние температуры на котрансляционное сворачивание люциферазы
- 4. 2. Влияние скорости синтеза люциферазы на эффективность её котрансляционного сворачивания
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