Structure: the amphipathic helix
LL-37 is usually drawn as an amphipathic alpha-helix, charged residues on one face and greasy residues on the other.
How 37 residues fold into a membrane-breaking tool
LL-37 is usually drawn as an amphipathic alpha-helix, charged residues on one face and greasy residues on the other. This unit builds that picture from what was actually measured: the helix lying flat on a bilayer in oriented-membrane NMR, the way LL-37 is carved out of hCAP-18 by proteolysis, and the family of shorter peptides the same precursor yields.
One warning sets the tone. The amphipathic helix was a prediction from sequence in the paper that opened this field, made for the 39-residue form it described, and the one structural measurement behind this unit is the oriented-bilayer NMR. The residue sequence and a solution helical content are on record; a net charge figure for LL-37 is not, so this unit describes the charge without printing a number for it.