51. 'Fuzzy oil drop' model applied to individual small proteins built of 70 amino acids
- Author
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Irena Roterman, Kinga Sałapa, Katarzyna Prymula, Department of Bioinformatics, Telemedicine Jagiellonian University - Collegium Medicum, Faculty of Chemistry, and Uniwersytet Jagielloński w Krakowie = Jagiellonian University (UJ)
- Subjects
Models, Molecular ,Serine Proteinase Inhibitors ,Protein Conformation ,030303 biophysics ,Protein Data Bank (RCSB PDB) ,biological activity ,small proteins ,Biology ,Catalysis ,Active site recognition ,Inorganic Chemistry ,03 medical and health sciences ,Structure-Activity Relationship ,Antifreeze protein ,Antifreeze Proteins ,active site recognition ,Physical and Theoretical Chemistry ,Amino Acids ,Databases, Protein ,Hydrophobicity scales ,hydrophobicity deficiency ,030304 developmental biology ,chemistry.chemical_classification ,0303 health sciences ,Binding Sites ,Functional analysis ,Biological activity ,Organic Chemistry ,Computational Biology ,Proteins ,Small proteins ,Computer Science Applications ,Amino acid ,Protein Structure, Tertiary ,Molecular Weight ,Computational Theory and Mathematics ,chemistry ,Biochemistry ,Protein body ,Proteins of unknown function ,proteins of unknown function ,Growth Hormone ,Hydrophobicity deficiency ,Hydrophobic and Hydrophilic Interactions ,Function (biology) ,Algorithms ,Molecular Chaperones ,Protein Binding - Abstract
International audience; The proteins composed of short polypeptides (about 70 amino acid residues) representing the following functional groups (according to PDB notation): growth hormones, serine protease inhibitors, antifreeze proteins, chaperones and proteins of unknown function, were selected for structural and functional analysis. Classification based on the distribution of hydrophobicity in terms of deficiency/excess as the measure of structural and functional specificity is presented. The experimentally observed distribution of hydrophobicity in the protein body is compared to the idealized one expressed by a three-dimensional Gauss function. The differences between these two distributions reveal the specificity of structural/functional characteristics of the protein. The residues of hydrophobicity deficiency versus the idealized distribution are assumed to indicate cavities with the potential to bind ligands, while the residues of hydrophobicity excess are interpreted as potentially participating in protein-protein complexation. The distribution of hydrophobicity irregularity seems to be specific for particular structures and functions of proteins. A comparative analysis of such profiles is carried out to identify the potential biological activity of proteins of unknown function.
- Published
- 2009