Abstract
Gramicidin A is a hydrophobic peptide antibiotic produced by Bacillus brevis. This membrane protein, consisting of alternating L- and D- amino acids, forms an ion channel that is selective for small univalent cations. The orientation of this peptide and its head-to-head dimer formation are of special interest. This can be studied via synthetic polymer membranes and EPR spectroscopy. Diblock and triblock copolymers are used as mimetic systems in place of lipid bilayers. CW-EPR spectroscopy coupled with site directed spin labeling (SDSL) can provide important structural information that is traditionally difficult to obtain in systems such as biological membranes.
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