The advantageous effect of flexibility in the binding of intrinsically disordered proteins has been theoretically predicted before as a ����fly-casting���� mechanism , and suggested for multi-domain proteins with long semi-flexible linkers and protein-binding function based on structural and dynamics studies . This tentative mode of operation for ABT-199 Bcl-2 inhibitor Harakiri agrees with the recently proposed ����membrane-embedded-together���� model for apoptotic mechanisms , which emphasizes that many interactions within the Bcl-2 family occur only in the membrane. Targeting of proteins to specific destinations at the appropriate time is crucial for cell function. This process often involves specific protein motifs, and requires the intricate regulation and coordination of different cellular components. Protein targeting is involved in prokaryotic cell division, during which a series of proteins are assembled in a hierarchical order to form a division septum at the correct mid-cell position. An essential component of the division apparatus is the tubulin homolog FtsZ; this is precisely located at the midpoint of the cell, where it forms a ring-like structure underneath the membrane and recruits other division proteins . In Escherichia coli , the NVP-BKM120 PI3K inhibitor position of the FtsZ ring is regulated by the Min system , which is composed of three proteins, MinC, MinD, and MinE; these cooperate to form a dynamic oscillator that guides the placement of the FtsZ assembly. MinC is a negative regulator of the FtsZ ring , and MinD associates with the cell membrane and undergoes a pole-to-pole oscillatory localization cycle in the presence of MinE and ATP . The Min system is a simple but dynamic and functional unit that has received attention from researchers involved in a variety of scientific disciplines . However, the underlying mechanisms responsible for the membrane-association properties of the Min system require further investigation. Correct functioning of the Min system involves the formation of membrane-associated polymeric structures of MinD . MinD accumulates in the membrane at a polar zone at one end of the cell. It associates with the cell membrane as a MinD-ATP complex through its C-terminal amino acids, which fold into an amphipathic helix .