A recent study shows that these basic residues are involved in actin binding.
Also noticeable is that by substituting R and A groups with hydrophobic and basic residues would give a potent compound.
It is a 42-long polypeptide containing 11 basic residues (9 lysines, 2 arginines) and 6 cysteines.
The outer surface of the β sheet also has many conserved hydrophobic and basic residues.
The opening of the cleft is lined by several highly conserved basic residues: Arg146, Arg221, and Lys229.
The two share a conserved basic residue that is present immediately prior to strand 4.
Near the C-terminus there is a positively charged surface formed by conserved basic residues, which is thought to interact with an ion channel.
Drosophila ribosomal protein S2 has 267 aminoacids and contains clustered basic residues.
It appears that the conserved basic residues, and not the zinc fingers, are important for complex formation.
These intermediates are then cleaved by CPE to remove the basic residues.
