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It is noteworthy that the minimum hydrophobic element for robust early recruitment of SRP is longer than the 7 to 9 hydrophobic residues within most cleavable N-terminal signal peptides (von Heijne, 1990).
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A hydrophobic element inserts into and bends membranes, and is conserved in pleckstrin homology domains of CERT and OSBP proteins.
Protein-based pharmacophores are shown as lines for hydrogen bond donor/acceptor and small green spheres for hydrophobic elements.
The retained hydrophobic elements were eluted from the XAD2 column with methanol, and from active charcoal with methanol, ethyl acetate or hexane.
When hydrophobic elements are exposed on the surface of a protein, they may interact with hydrophobic elements of other proteins to escape the aqueous environment.
Newly exposed hydrophobic elements, shielded by chaperones such as HSP70 and HSP40, are transiently protected from reaggregation.
When multiple such surface-exposed hydrophobic elements are present, the potential exists for protein aggregation, forming insoluble aggregates that are often toxic to cells [26].
This flexibility may permit sampling of the lipid bilayer by the translocating nascent chain, thereby allowing suitably hydrophobic elements to insert in the membrane.
Figure 4 Minimum elements corresponding different initial elements.
The collection of all smallest elements (minimum elements) of A is denoted by minA.
This shows that the minimum element is unique.
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