Folding-unfolding energy change of a simple sphere model protein and an energy landscape of the folding process.
We have calculated the free energy of a spherical model of a protein or part of a protein generated in the way of protein folding. Two spherical models are examined; one is a homogeneous model consisting of only one residue type--hydrophobic. The other is a heterogeneous model consisting of two residue types--strong hydrophobic and weak hydrophobic. Both models show a folding transition state, and the latter model reproduces the trend of the experimental folded-unfolded energy change. The heterogeneous model suggests that in the folding process of a protein of more than 70 residues, a specific region of the protein folds first to form a stable region, then the other residues follow the folding process. The energy landscape of folding of a small protein is approximately a funnel model, whereas a flatter energy landscape is suggested for larger proteins of more than 55-70 residues.
Fukunishi
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Department of Chemistry, Rutgers, the State University of New Jersey, Piscataway, USA. fukunisi@rtc.riken.go.jp
D004735:Energy Transfer; D008432:Mathematical Computing; D017510:Protein Folding