Sequence-dependence of secondary structure formation. III: β-structure forming potential of amphiphilic oligopeptides containing alternating L-Val-L-Thr and L-Leu-L-Ser residues
The conformational behaviour of the monodisperse amphiphilic oligopeptides (L-Thr-L-Val) sub(n) (I and II) and (L-Ser-L-Leu) sub(n) (III) for n = 1-4 was investigated by CD spectroscopy in TFE, MeOH and water. The use of amphiphilic peptides for the construction of artificial proteins is briefly dis...
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Veröffentlicht in: | International journal of peptide and protein research 1986, Vol.27 (3), p.314-319 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The conformational behaviour of the monodisperse amphiphilic oligopeptides (L-Thr-L-Val) sub(n) (I and II) and (L-Ser-L-Leu) sub(n) (III) for n = 1-4 was investigated by CD spectroscopy in TFE, MeOH and water. The use of amphiphilic peptides for the construction of artificial proteins is briefly discussed. |
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ISSN: | 0367-8377 |