Conformation of naturally-occurring peptides in surfactant solution: Its relation to the structure-forming potential of amino acid sequence
Short polypeptides are unordered in aqueous solution. Surfactants provide a proteinaceous environment in which ordered conformation of the peptides can be induced if they have a structure-forming potential. Ten peptides studied are classified into four types: (I) helix-forming, (II) β-forming, (III)...
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Veröffentlicht in: | Biochemical and biophysical research communications 1978-05, Vol.82 (1), p.85-91 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Short polypeptides are unordered in aqueous solution. Surfactants provide a proteinaceous environment in which ordered conformation of the peptides can be induced if they have a structure-forming potential. Ten peptides studied are classified into four types: (I) helix-forming, (II) β-forming, (III) either helix- or β-forming, and (IV) neither structure-forming. At low molar ratio, R, of sodium dodecyl sulfate to peptide (residue) (R < 10), type II peptides appear to be aggregated, but they dissociate at R ≅ 100 or more. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(78)90580-6 |