Mutual Synergetic Folding (MSF) proteins belong to a recently discovered class of
proteins. These proteins are disordered in their monomeric but ordered in their oligomeric
forms. Their amino acid composition is more similar to globular proteins than to disordered
ones. Our preceding work shed light on important structural aspects of the structural
organization of these proteins, but the background of this behavior is still unknown.
We suggest that solvent accessibility is an important factor, especially solvent accessibility
of the peptide bonds can be accounted for this phenomenon. The side chains of the
amino acids which form a peptide bond have a high local contribution to the shielding
of the peptide bond from the solvent. During the oligomerization step, other non-local
residues contribute to the shielding. We investigated these local and non-local effects
of shielding based on Shannon information entropy calculations. We found that MSF
and globular homodimeric proteins have different local contributions resulting from
different amino acid pair frequencies. Their non-local distribution is also different
because of distinctive inter-subunit contacts.
