Importance of tryptophan dipoles for protein function: 5-fluorination of tryptophans in gramicidin A channels
Andersen OS, Greathouse DV, Providence LL, Becker MD, Koeppe RE II 1998 Importance of tryptophan dipoles for protein function: 5-fluorination of tryptophans in gramicidin A channels. J Am Chem Soc 120:5142-5146
Gramicidin A transmembrane ion-channel. Three-dimensional structure reconstruction based on NMR spectroscopy and energy refinement
USSR
Arseniev AS, Lomize AL, Barsukov IL, Bystrov VF 1986 Gramicidin A transmembrane ion-channel. Three-dimensional structure reconstruction based on NMR spectroscopy and energy refinement. Biol Membr (USSR) 3:1077-1104
Structure of the gramicidin A channel: Discrimination between the π-L,D and the beta-helix by electrical measurements with lipid bilayer membranes
Bamberg E, Apell HJ, Alpes HJ 1977 Structure of the gramicidin A channel: discrimination between the π-L,D and the beta-helix by electrical measurements with lipid bilayer membranes. Proc Natl Acad Sci USA 74:2402-2406
Amino acid sequence modulation of gramicidin channel function: Effects of tryptophan-to-phenylalanine substitutions on the single-channel conductance and duration
Becker MD, Greathouse DV, Koeppe RE II, Andersen OS 1991 Amino acid sequence modulation of gramicidin channel function: effects of tryptophan-to-phenylalanine substitutions on the single-channel conductance and duration. Biochemistry 30:8830-8839
The conducting form of gramicidin A is a right-handed double-stranded double helix
Burkhart BM, Li N, Langs DA, Pangborn WA, Duax WL 1998 The conducting form of gramicidin A is a right-handed double-stranded double helix. Proc Natl Acad Sci USA 95:12950-12955