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Titin I27: A Protein with a Complex Folding Landscape

Author: Jane Clarke
Publisher: London : Henry Stewart Talks, 2007.
Series: Henry Stewart talks., Biomedical & life sciences collection., Protein folding, aggregation and design: concepts, experiments, theories and mechanisms.
Edition/Format:   eVideo : EnglishView all editions and formats
Database:WorldCat
Summary:
Audio-visual presentation : Examination of the folding of titin 127 ; Evolution of the protein to withstand stress from mutation, the environment and to withstand mechanical force in the muscle ; Use of a combination of protein engineering, kinetic and thermodynamic measurements, computer simulations and single molecule atomic force microscopy to understand how evolution acts on protein sequences to allow them to  Read more...
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Details

Material Type: Internet resource, Videorecording
Document Type: Internet Resource, Computer File, Visual material
All Authors / Contributors: Jane Clarke
OCLC Number: 652446279
Notes: Streaming video : (38:14 : sd., col.).
Title from header on screen (viewed Jan. 21, 2008).
Details: System requirements: Operating System: PC Windows 2000+, Mac OSX+ 3.2. Browser Compatibility: IE6+, Firefox 2+, Opera 9+, Safari 2+ 3.3. Browser settings: enable JavaScript, enable popups from the Henry Stewart Talks site. 3.4. Required Browser Plugins & Viewers: Adobe (Macromedia) Flash Player 7+, Adobe Acrobat Reader 6.0+; Mode of access: World Wide Web.
Series Title: Henry Stewart talks., Biomedical & life sciences collection., Protein folding, aggregation and design: concepts, experiments, theories and mechanisms.
Responsibility: Jane Clarke.

Abstract:

Audio-visual presentation : Examination of the folding of titin 127 ; Evolution of the protein to withstand stress from mutation, the environment and to withstand mechanical force in the muscle ; Use of a combination of protein engineering, kinetic and thermodynamic measurements, computer simulations and single molecule atomic force microscopy to understand how evolution acts on protein sequences to allow them to adapt to stressful conditions, probably explaining why immunoglobulin-like proteins are used so successfully in evolution to perform a number of functions.

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