Solubility and Aggregation of Selected Proteins Interpreted on the Basis of Hydrophobicity Distribution.

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 observed in the protein to a f

SUBMITTER: Ptak-Kaczor M 

PROVIDER: S-EPMC8125953 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature