It has been reported that the size of the pores punctured by perforins are relatively small (around 16 nM in diameter), which may not allow protein molecules to freely pass through [14].
Detailed knowledge of a pharmacophore map may also allow protein function prediction or provide support for human-generated binding hypotheses.
Hence the short length of JmjC domain may allow JmjC proteins to evolve new functions quickly by combining with new domains, which can promote protein-protein interaction, DNA binding or recognition of chromatin modification.
First, mitochondrial proteins are prestin partners because the OHC's unique cellular structure may allow mitochondrial proteins to be inserted into cellular membranes.
Additional interactions of the protein with headgroups of annular lipids, that is, lipid-binding sites, may allow membrane proteins to select for specific lipids and/or to form tight interactions with lipids important for their function or structural integrity.
The large number of family members may allow these proteins to assume a repertoire of functions, or ensure redundancy between family members during development.
Therefore, the generation of ceramide may allow these proteins, which are cytoplasmic or loosely associated with the outer mitochondrial membrane in viable cells, to change their conformation, integrate into the membrane, and cause apoptosis.
This larger disordered region may allow the protein to maintain a similar conformation for the structural regions that are associated with RNA genome.
The ability of DCs to carry antigen for presentation to T cells may allow F protein to directly inhibit T cell proliferation.
