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The C1 domains of classical and novel PKCs mediate their diacylglycerol-dependent translocation. Using fluorescence resonance energy transfer, we studied the contribution of different negatively charged phospholipids and diacylglycerols to membrane binding. Three different C1B domains of PKCs were studied (the classical γ, and the novel δ and ɛ), together with different lipid mixtures containing three...
Bak is a pro-apoptotic protein widely distributed in different cell types that is associated with the mitochondrial outer membrane, apparently through a C-terminal hydrophobic domain. We used infrared spectroscopy to study the secondary structure of a synthetic peptide (+3HN-188ILNVLVVLGVVLLGQFVVRRFFKS211-COO–) with the same sequence as the C-terminal domain of Bak. The spectrum of this peptide...
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