Int. J. Mol. Sci. 2009, 10(3), 844-861; doi:10.3390/ijms10030844
Article

Chaperonin Structure - The Large Multi-Subunit Protein Complex

1,2email, 2,3email and 1,2,* email
Received: 9 February 2009; in revised form: 23 February 2009 / Accepted: 26 February 2009 / Published: 2 March 2009
(This article belongs to the Special Issue Protein Folding)
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Abstract: 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.
Keywords: Protein folding; hydrophobicity; chaperonin
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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.

AMA Style

Banach M, Stąpor K, Roterman I. Chaperonin Structure - The Large Multi-Subunit Protein Complex. International Journal of Molecular Sciences. 2009; 10(3):844-861.

Chicago/Turabian Style

Banach, Mateusz; Stąpor, Katarzyna; Roterman, Irena. 2009. "Chaperonin Structure - The Large Multi-Subunit Protein Complex." Int. J. Mol. Sci. 10, no. 3: 844-861.


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