How proteins adapt to a membrane-water interface.

By J. Killian, Gunnar von Heijne. TIBS -Trends in Biochemical Sciences. Regular ed, 2000

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Topology Prediction of α-Helical Transmembrane Proteins (2016, background): “actions with lipid head groups are shown to stabilize the structure [39].”
Bilayer thickness and membrane protein function: an energetic perspective. (2007, background): “Peptides lacking polar/charged anchors tend to have only little influence on the lipid phase behavior (54, 57).”
Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes (2004, background): “The interface with HDL was further defined by a characteristic 'aromatic belt' rich in tryptophan and tyrosine side chains, and by a lysine side chain on H1 (ref”
Cell‐penetrating peptides: 20 years later, where do we stand? (2013, background): “strated to have favorable free energies of insertion into the bilayer interface [106,107].”