Chaperonin structure: the large multi-subunit protein complex.
The multi sub-unit protein structure representing the chaperonins group is analyzed with respect to its hydrophobicity distribution. The proteins of this group assist protein folding supported by ATP. The specific axial symmetry GroEL structure (two rings of seven units stacked back to back - 524 aa each) and the GroES (single ring of seven units - 97 aa each) polypeptide chains are analyzed using the hydrophobicity distribution expressed as excess/deficiency all over the molecule to search for structure-to-function relationships. The empirically observed distribution of hydrophobic residues is confronted with the theoretical one representing the idealized hydrophobic core with hydrophilic residues exposure on the surface. The observed discrepancy between these two distributions seems to be aim-oriented, determining the structure-to-function relation. The hydrophobic force field structure generated by the chaperonin capsule is presented. Its possible influence on substrate folding is suggested.
Banach
Mateusz
M
Department of Bioinformatics and Telemedicine - Jagiellonian University, Collegium Medicum, Lazarza 16, 31-531 Krakow, Poland.|Faculty of Physics, Astronomy and Applied Computer Science - Jagiellonian University, Reymonta 4, 30-059 Krakow, Poland.
Stąpor
Katarzyna
K
Faculty of Physics, Astronomy and Applied Computer Science - Jagiellonian University, Reymonta 4, 30-059 Krakow, Poland.|Silesian Technical University, Institute of Computer Science, Akademicka 16 44-100 Gliwice, Poland.
Roterman
Irena
I
Department of Bioinformatics and Telemedicine - Jagiellonian University, Collegium Medicum, Lazarza 16, 31-531 Krakow, Poland.|Faculty of Physics, Astronomy and Applied Computer Science - Jagiellonian University, Reymonta 4, 30-059 Krakow, Poland.
D018835:Chaperonin 10 / Q000737:chemistry / Q000378:metabolism; D018834:Chaperonin 60 / Q000737:chemistry / Q000378:metabolism; D018833:Chaperonins / Q000737:chemistry* / Q000378:metabolism; D016000:Cluster Analysis; D057927:Hydrophobic and Hydrophilic Interactions; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism
D018835:Chaperonin 10; D018834:Chaperonin 60; D021122:Protein Subunits; D018833:Chaperonins