ISSN:
1432-1017
Keywords:
Linear gramicidins
;
Monolayers
;
Infrared spectroscopy
;
Conformational analysis
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Physics
Notes:
Abstract A comparative monolayer and infrared study of analogues of gramicidin A containing either tyrosines or naphthylalanines instead of tryptophans indicates that the nature of the aromatic residues influences the favoured conformation of the peptides. Polar residues favour the single stranded ΠDL helix while non polar residues favour the double stranded helix. For partly tryptophan to naphthylalanine substituted analogues the positions of the substitutions orientate the favored conformation. The nature of these substitutions may also modify the peptide-lipid interactions.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00180165
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