How proteins specifically localize to the phospholipid monolayer surface of lipid droplets
(LDs) is being unraveled. We review here the major known pathways of protein targeting to …

Antimicrobial peptides encompass a wide variety of structural motifs. Many peptides have α-
helical structures. The majority of these peptides are cationic and amphipathic but there are …

Numerous data have been collected on lipid-binding amphipathic helices involved in
membrane-remodeling machineries and vesicular transport. Here we describe how, with …

In the last 20 years, an increasing number of studies have been reported on membrane
active peptides. These peptides exert their biological activity by interacting with the cell …

Bacteria and eukaryotic cells contain geometry-sensing tools in their cytosol: protein motifs
or domains that recognize the curvature, concave or convex, deep or shallow, of lipid …

Membrane proteins present a hydrophobic surface to the surrounding lipid, whereas
portions protruding into the aqueous milieu expose a polar surface. But how have proteins …

Abstract The Golgi-associated protein ArfGAP1 has an unusual membrane-adsorbing
amphipathic α-helix: its polar face is weakly charged, containing mainly serine and …

There is general consensus that amphipathic α-helices and β sheets represent the major
lipid-associating motifs of apolipoprotein (apo) B-100. In this review, we examine the …

Amphipathic helices (AHs), a secondary feature found in many proteins, are defined by their
structure and by the segregation of hydrophobic and polar residues between two faces of …

Tryptophan fluorescence is a powerful tool for studying protein structure and function,
especially membrane-active proteins and peptides. It is arguably the most frequently used …