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Results reveal that amide-to-ester substitution in the gramicidin channel protein removes the hydrogen bond involved in the intramolecular stabilization between Gly and Val of N- and C-termini, respectively. Data further show that the substitution alters the charge distribution leading to intermolecular hydrogen bond disruption and subunit association and dissociation.

The D-Leu(super 10) residue creates the optimal orientation of Trp(super 9) in gramicidin channels in lipid bilayers. Gramicidin A has four Trp residues, which are essential for channel assembly and stability and ion transport.

A study was conducted to analyze the importance of the spacer residues between the tryptophans in gramicidin A for channel structure and function. The Jasco J-710 circular dichroism spectrometer was utilized to determine CD spectra between 22 to 24 degrees C. Experimental results indicated that the stereochemistry of the aliphatic residues between the tryptophans of gramicidin A are critical for channel structure and function.

Investigates the importance of the `spacer' residues between the tryptophans in gramicidin A (gA) for channel structure and function. Material and methods of the study; Results of the study; Discussion on the results.