title: Hydrophobic core in domains of immunoglobulin-like fold.
abstract: This work analyzes proteins which contain an immunoglobulin fold, focusing on their hydrophobic core structure. The "fuzzy oil drop" model was used to measure the regularity of hydrophobicity distribution in globular domains belonging to proteins which exhibit the above-mentioned fold. Light-chain IgG domains are found to frequently contain regular hydrophobic cores, unlike the corresponding heavy-chain domains. Enzymes and DNA binding proteins present in the data-set are found to exhibit poor accordance with the hydrophobic core model.
authors.affiliation: a Department of Bioinformatics and Telemedicine , Collegium Medicum, Jagiellonian University , Krakow , Poland .
authors.forename: M
authors.initials: M
authors.lastname: Banach
authors.forename: I
authors.initials: I
authors.lastname: Roterman
authors.forename: N
authors.initials: N
authors.lastname: Prudhomme
authors.forename: J
authors.initials: J
authors.lastname: Chomilier
mesh_terms: D004268:DNA-Binding Proteins / Q000737:chemistry; D030562:Databases, Protein; D004798:Enzymes / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D007136:Immunoglobulins / Q000737:chemistry*; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D004268:DNA-Binding Proteins; D004798:Enzymes; D007136:Immunoglobulins
keywords: hydrophobicity; hydrophobicity density; immunoglobulin fold; tertiary structure