Computational analysis of the conformational behavior of representative peptides identified four distinct backbone conformations, each associated with the membrane-binding properties of the peptides. Two of them, fold1-4 and fold2-6, determine the general shape of the molecule backbone, while the other two, flat and bend, characterize the shape and plasticity of the surface hydrophobic patch formed by both the backbone and side chains. Depending on the population ratio within the types of these conformations, each cyclic peptide can be classified into one of four classes, as shown in Figure .