International Journal of Molecular Sciences Article Solubility and Aggregation of Selected Proteins Interpreted on the Basis of Hydrophobicity Distribution Magdalena Ptak-Kaczor 1,2, Mateusz Banach 1 , Katarzyna Stapor 3 , Piotr Fabian 3 , Leszek Konieczny 4 and Irena Roterman 1,2,* 1 Department of Bioinformatics and Telemedicine, Jagiellonian University—Medical College, Medyczna 7, 30-688 Kraków, Poland;
[email protected] (M.P.-K.);
[email protected] (M.B.) 2 Faculty of Physics, Astronomy and Applied Computer Science, Jagiellonian University, Łojasiewicza 11, 30-348 Kraków, Poland 3 Institute of Computer Science, Silesian University of Technology, Akademicka 16, 44-100 Gliwice, Poland;
[email protected] (K.S.);
[email protected] (P.F.) 4 Chair of Medical Biochemistry—Jagiellonian University—Medical College, Kopernika 7, 31-034 Kraków, Poland;
[email protected] * Correspondence:
[email protected] Abstract: Protein solubility is based on the compatibility of the specific protein surface with the polar aquatic environment. The exposure of polar residues to the protein surface promotes the protein’s solubility in the polar environment. The aquatic environment also influences the folding process by favoring the centralization of hydrophobic residues with the simultaneous exposure to polar residues. The degree of compatibility of the residue distribution, with the model of the concentration of hydrophobic residues in the center of the molecule, with the simultaneous exposure of polar residues is determined by the sequence of amino acids in the chain. The fuzzy oil drop model enables the quantification of the degree of compatibility of the hydrophobicity distribution Citation: Ptak-Kaczor, M.; Banach, M.; Stapor, K.; Fabian, P.; Konieczny, observed in the protein to a form fully consistent with the Gaussian 3D function, which expresses L.; Roterman, I.