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

International Journal of Molecular Sciences

Leszek Konieczny¹  Irena Roterman²  Magdalena Ptak-Kaczor²  Mateusz Banach²  Katarzyna Stapor³  Piotr Fabian³ 

[1] Chair of Medical Biochemistry—Jagiellonian University—Medical College, Kopernika 7, 31-034 Kraków, Poland;Department of Bioinformatics and Telemedicine, Jagiellonian University—Medical College, Medyczna 7, 30-688 Kraków, Poland;Institute of Computer Science, Silesian University of Technology, Akademicka 16, 44-100 Gliwice, Poland;

关键词: solubility;    complexation;    hydrophobicity;    antifreeze;    pilin;    protein structure;   

DOI  :  10.3390/ijms22095002

来源: DOAJ

【 摘 要 】

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 form fully consistent with the Gaussian 3D function, which expresses an idealized distribution that meets the preferences of the polar water environment. The varied degrees of compatibility of the distribution observed with the idealized one allow the prediction of preferences to interactions with molecules of different polarity, including water molecules in particular. This paper analyzes a set of proteins with different levels of hydrophobicity distribution in the context of the solubility of a given protein and the possibility of complex formation.

【 授权许可】

Unknown