Metamorphic response of the CLIC1 chloride intracellular ion channel protein upon membrane interaction

The insights into the chloride intracellular channel (CLIC) transmembrane form are obtained by fluorescence resonance energy transfer (FRET) spectroscopy. The studies have shown a large conformational unfolding occurring between the N- and C-domains of CLIC1 upon interaction with the membrane, where the N-terminal domain of CLIC1 has inserted into the lipid bilayer, while the C-domain has remained in solution on the extravesicular side of the membrane.