Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins

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.

On Small Complete Sets of Functions

Using Local Residues and the Duality Principle a multidimensional variation of the completeness theorems by T. Carleman and A. F. Leontiev is proven for the space of holomorphic functions defined on a suitable open strip Tα ⊂ C2. The completeness theorem is a direct consequence of the Cauchy Residue Theorem in a torus. With suitable modifications the same result holds in Cn.