Abstract
Membrane-bound proteins (MBPs) have immense significance because they perform inherently refractory to isolation and to structural and functional characterization due to the instability of their hydrophobic domains outside of their native membranes. At the leading edge of membrane research are styrene-maleic acid (SMA) polymers that encapsulate membrane protein complexes into SMA lipoprotein particles (SMALPs) in their native and functionally active states. In this study, we employed an approach where we used reductionist and mitochondrial systems in tandem to elucidate conditions for optimal SMA extraction.
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