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Open AccessArticle

Chaperonin Structure - The Large Multi-Subunit Protein Complex

1
Department of Bioinformatics and Telemedicine – Jagiellonian University, Collegium Medicum, Lazarza 16, 31-531 Krakow, Poland
2
Faculty of Physics, Astronomy and Applied Computer Science - Jagiellonian University, Reymonta 4, 30-059 Krakow, Poland
3
Silesian Technical University, Institute of Computer Science, Akademicka 16 44-100 Gliwice, Poland
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2009, 10(3), 844-861; https://doi.org/10.3390/ijms10030844
Received: 9 February 2009 / Revised: 23 February 2009 / Accepted: 26 February 2009 / Published: 2 March 2009
(This article belongs to the Special Issue Protein Folding 2009)
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. View Full-Text
Keywords: Protein folding; hydrophobicity; chaperonin Protein folding; hydrophobicity; chaperonin
MDPI and ACS Style

Banach, M.; Stąpor, K.; Roterman, I. Chaperonin Structure - The Large Multi-Subunit Protein Complex. Int. J. Mol. Sci. 2009, 10, 844-861.

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