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Folding‐unfolding energy change of a simple sphere model protein and an energy landscape of the folding process
Author(s) -
Fukunishi Yoshifumi
Publication year - 1998
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(19981115)33:3<408::aid-prot9>3.0.co;2-2
Subject(s) - lattice protein , folding funnel , energy landscape , downhill folding , protein folding , phi value analysis , contact order , folding (dsp implementation) , funnel , chemical physics , chemistry , crystallography , biophysics , biology , biochemistry , organic chemistry , electrical engineering , engineering
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. Proteins 33:408–416, 1998. © 1998 Wiley‐Liss, Inc.