Clarke, Jane.
Titin 127 a protein with a complex folding landscape / [electronic resource] : Jane Clarke. - London : Henry Stewart Talks, 2007. - 1 online resource (1 streaming video file (38 min.) : color, sound). - Protein folding, aggregation and design : concepts, experiments, theories and mechanisms, 2056-452X . - Henry Stewart talks. Biomedical & life sciences collection. Protein folding, aggregation and design : concepts, experiments, theories and mechanisms. .
Animated audio-visual presentation with synchronized narration. Title from title frames.
Contents: 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.
Access restricted to subscribers.
Mode of access: World Wide Web.
1279 Henry Stewart Talks
Muscle Proteins.
Protein Conformation.
Protein Folding.
Protein Kinases.
Proteins.
Titin 127 a protein with a complex folding landscape / [electronic resource] : Jane Clarke. - London : Henry Stewart Talks, 2007. - 1 online resource (1 streaming video file (38 min.) : color, sound). - Protein folding, aggregation and design : concepts, experiments, theories and mechanisms, 2056-452X . - Henry Stewart talks. Biomedical & life sciences collection. Protein folding, aggregation and design : concepts, experiments, theories and mechanisms. .
Animated audio-visual presentation with synchronized narration. Title from title frames.
Contents: 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.
Access restricted to subscribers.
Mode of access: World Wide Web.
1279 Henry Stewart Talks
Muscle Proteins.
Protein Conformation.
Protein Folding.
Protein Kinases.
Proteins.