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Titin I27 : a protein with a complex folding landscape / Jane Clarke.
- Format:
- Video
- Author/Creator:
- Clarke, Jane, author.
- Language:
- English
- Subjects (All):
- Proteins--Conformation.
- Proteins.
- Physical Description:
- 1 online resource (1 streaming video file (38 min.)) : sound, color
- Other Title:
- Titin I27
- Place of Publication:
- London : Henry Stewart Talks Ltd, 2007.
- System Details:
- video file
- Contents:
- Introduction
- Titin I27 - general description
- Folding - unfolding plot for Titin I27
- Environmental conditions change folding pathway
- TI27 mutants - unfolding pathways
- Parallel folding pathways
- How can we analyze these data?
- High and low-stress unfolding pathway
- Temperature can change the unfolding pathway
- Mutations can change the folding pathway
- Titin - a protein experiencing mechanical stress
- Titin - effects of force
- How does Titin resist unfolding under stress?
- Addition of force lowers the unfolding energy barrier
- Using AFM to investigate protein unfolding
- First experiments - using whole proteins
- The ideal protein - 8 repeats of I27
- The protein - 8 repeats of I27 - unfolding
- AFM experiments let comparison with simulations
- Simulations - first step - forming an intermediate
- Humps appear on the plot of unfolding
- Mutation in the A-strand does not affect unfolding
- A-strand lacking intermediate is stable
- TI I27 has an intermediate on the unfolding pathway
- Protein engineering for analysis of unfolding
- Rationale
- Different mutanst affect the folding force differently
- Titin forced unfolding pathway
- TS under force vs. physiological conditions
- What can alter the protein unfolding landscape
- Single molecular experiments let us see rare events
- How do multi-domain proteins avoid aggregation
- Tandem proteins aggregate faster
- Strategies of aggregation avoidance
- Titin domains behave independently
- Strategy 2 - weak modules next to strong modules
- Strategy 3 - select for certain residues
- Removing the prolines speeds up aggregation
- Strategy 4 - diversify the sequence of domains (1)
- Strategy 4 - diversify the sequence of domains (2)
- Evolutionary pressure to diversify sequences
- How similar are Titin domains?
- Conclusion.
- Notes:
- Description based on publisher supplied metadata and other sources.
- Retrieved April 13, 2024, from https://hstalks.com/bs/432/.
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