[1][2][3] Their tertiary structure is usually maintained by disulphide bridges,[4] metal ligands,[5] and or cofactors such as heme.
Some small proteins serve important regulatory functions by direct interaction with certain enzymes and are therefore also an interesting tool for biotechnological applications in microorganisms.
For larger ORFs, computational identification is based solely on their long uninterrupted coding potential.
Computational searches for small proteins take into account multiple parameters, such as the presence of a ribosome binding site and amino acid conservation.
Binding of a ribosome on an mRNA suggests that the transcript is being actively translated, allowing for the identification even of very small ORFs.