The pairedless proteins possess molecular weights of 43, 33, or 32kDa, depending on the particular start codon used.

Both proteins possess neurotoxic, helmintho-toxic, and ribonucleo-lytic activities.

These transmembrane proteins possess a large number of alpha helices immersed in the lipid matrix.

Both thermal and chemical denaturation confirm that, all redesigned proteins, in agreement with the calculations, possess increased stability.

In eukaryotic cells, most intracellular proteins activated by a ligand/receptor interaction possess an enzymatic activity; examples include tyrosine kinase and phosphatases.

These proteins possess 16 strictly conserved cysteines and contain 8 disulfide bonds.

Ancestral moonlighting proteins originally possessed a single function but through evolution, acquired additional functions.

This protein possesses two ATP-hydrolyzing domains, which allows the protein to use energy in the form of ATP.

The protein has been predicted to localize in the nucleus, and possesses a cut signal peptide at amino acid 21.

However, a recent 3D study shows that these three proteins possess similar "sweet fingers" believed to elicit the sweet taste.