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The intracellular C-terminal domain (CTD) of KcsA, a bacterial homotetrameric potassium channel, is a 40-residue long segment which natively adopts a helical bundle conformation with four-fold symmetry. A hallmark of KcsA behavior is a pH-induced conformational change which leads to opening of the channel at acidic pH. While crystal structures of full-length KcsA failed to observe a pH-effect upon the CTD, other biophysical methods have presented evidence to the contrary. We approached the question of CTD structure and its pH-dependence by studying the behavior of soluble peptides corresponding to residues 128-160 of the CTD (CTD34).
|Original language||American English|
|State||Published - 2015|
|Event||59th Biophysical Society meeting - Baltimore, United States|
Duration: 7 Feb 2015 → 11 Feb 2015
|Conference||59th Biophysical Society meeting|
|Period||7/02/15 → 11/02/15|