Richard M. Epand

TL;DR: Direct imaging of the interaction of the apoptotic protein, Bax, with membrane bilayers shows the presence of toroidal-shaped pores using atomic force microscopy, which shows that Bax by itself can form pores in membrane bilayer.

TL;DR: Modeling studies indicate that several peptides with sequences related to LWYIK, a segment found in the gp41 protein of HIV and believed to play a role in sequestering this protein to a cholesterol-rich domain in the membrane, tend to partition with their mass center at the membrane interface at the level of the hydroxyl of cholesterol.

TL;DR: It is proposed that tafazzin reacts with non-bilayer-type lipid domains that occur in curved or hemifused membrane zones and that acyl specificity is driven by the packing properties of these domains.

TL;DR: It is proposed that the wedgeshape of class A helixes stabilizes membrane bilayers, whereas the inverted wedge shape of class L helIXes destabilizes membrane Bilayers, and, thus, one class will neutralize the effect of the other class on membranes.

TL;DR: Cholesterol can promote the insertion of N-acetyl-LWYIK-amide into a membrane and this peptide will sequester cholesterol into domains, which helps to explain the observation that this sequence is found to be important in causing the fusion protein of human immunodeficiency virus (HIV) to sequester into raft domains in biological membranes.