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Chaperonin Structure – The Large Multi-Subunit Protein Complex

By Mateusz Banach, Katarzyna Stąpor and Irena Roterman


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

Topics: Article
Publisher: Molecular Diversity Preservation International (MDPI)
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Provided by: PubMed Central

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  2. (1976). A simplified representation of protein conformations for rapid simulation of protein folding.
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  5. Algorithms for clustering data; Prentice Hall: Englewood Cliffs NJ,
  6. (2009). Chaperonin complex with a newly folded protein encapsulated in the folding chamber. Nature
  7. (2005). Chaperonin GroEL meets the substrate protein as a "load" of the rings.
  8. (2009). Fine structure analysis of a protein folding transition state; Distinguishing between hydrophobic stabilization and specific packing.
  9. (2006). Fuzzy oil drop hydrophobic force field - a model to represent late-stage folding (in silico) of lysozyme.
  10. (2006). Gauss-function-Based model of hydrophobicity density in proteins. Silico Biol.
  11. (1999). GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings Cell
  12. (1997). GroEL-mediated protein folding. Protein Sci.
  13. (1998). GroEL/GroES: Structure and function of a two-stroke folding machine.
  14. (2006). Hydrophobic collapse in (in silico) protein folding.
  15. (2006). Hydrophobic collapse in late-stage folding (in silico) of bovine pancreatic trypsin inhibitor. Biochimie
  16. (1985). Hydrophobicity of amino acid residues in globular proteins. Science
  17. (1986). Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins.
  18. Is the protein folding an aim-oriented process? Human haemoglobin as example.
  19. (2006). Ligation site in proteins recognized in silico. Bioinformation
  20. (2007). Localization of ligand binding site in proteins identified in
  21. Prediction of functional sites based on the fuzzy oil drop model.
  22. (1981). Prediction of protein antigenic determinants from amino acid sequences.
  23. (2006). Sequence-structure-function relation characterized in silico.
  24. (2004). Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.

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