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- W2080574127 abstract "Brownian dynamics simulation study of the folding of a model thermostable chicken villin head piece subdomain, a 36-residue protein (HP-36), is carried out using the hydropathy scale of amino acids. The diverse interactions among the amino acid residues are categorized into three classes by introducing a simplified hydrophobic scale. The simulations incorporate all the six different inter- and intraamino acid interactions. The model protein reproduces some of the qualitative features of the complex protein folding, including the funnel-like energy landscape. Although there are several states near the minimum of the folding funnel, we could identify a stable native configuration. In addition, the study reveals a correlation between the contact order, topology, and the stability." @default.
- W2080574127 created "2016-06-24" @default.
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- W2080574127 date "2002-04-29" @default.
- W2080574127 modified "2023-09-24" @default.
- W2080574127 title "Foldability and the funnel of HP-36 protein sequence: Use of hydropathy scale in protein folding" @default.
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- W2080574127 doi "https://doi.org/10.1063/1.1467341" @default.
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