ISSN:
1432-1017
Schlagwort(e):
Linear gramicidins
;
Analogues
;
Conductance
;
Dipole moment
;
Hydrophobicity
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
,
Physik
Notizen:
Abstract This paper describes the single channel properties of a series of synthetic analogues of gramicidin A, where all four tryptophans are replaced either by tyrosine or by several O-protected (benzyl, methyl, ethyl or t-butyl) derivatives. It is shown that, although all analogues bear similar dipole moment on their side-chains, the conductance depends on the hydrophobicity of these protecting groups. An analysis of the conductance data suggests that the conductance is governed by the binding process and a possible explanation, based on conformational considerations, is proposed.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00196918
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