The sequence determinants of amyloid fibril formation [electronic resource] / Fabrizio Chiti.

By: Chiti, Fabrizio [spk]Material type: FilmFilmSeries: Henry Stewart talksBiomedical & life sciences collection. Protein folding, aggregation and design : concepts, experiments, theories and mechanisms: Publisher: London : Henry Stewart Talks, 2007Description: 1 online resource (1 streaming video file (35 min.) : color, sound)Subject(s): Amyloid | Protein Conformation | Protein Folding | ProteinsOnline resources: Click here to access online | Series
Contents:
Contents: Amyloid fibril formation is a shared property of proteins -- The effect of mutations on the aggregation of unstructured polypeptide chains -- The importance of hydrophobicity, propensity to form beta-sheet structure and charge in amyloid formation of unstructured proteins -- The regions of the sequence forming the beta-core of amyloid fibrils -- The sequence and structural determinants of aggregation for partially folded states of proteins -- Amino acid sequences have evolved to avoid formation of amyloid-like aggregates.
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Animated audio-visual presentation with synchronized narration.

Title from title frames.

Contents: Amyloid fibril formation is a shared property of proteins -- The effect of mutations on the aggregation of unstructured polypeptide chains -- The importance of hydrophobicity, propensity to form beta-sheet structure and charge in amyloid formation of unstructured proteins -- The regions of the sequence forming the beta-core of amyloid fibrils -- The sequence and structural determinants of aggregation for partially folded states of proteins -- Amino acid sequences have evolved to avoid formation of amyloid-like aggregates.

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