Sequence-based study of two related proteins with different folding behaviors |
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Authors: | Favrin Giorgio Irbäck Anders Wallin Stefan |
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Institution: | Complex Systems Division, Department of Theoretical Physics, Lund University, Lund, Sweden. |
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Abstract: | Z(SPA-1) is an engineered protein that binds to its parent, the three-helix-bundle Z domain of staphylococcal protein A. Uncomplexed Z(SPA-1) shows a reduced helix content and a melting behavior that is less cooperative, compared with the wild-type Z domain. Here we show that the difference in folding behavior between these two sequences can be partly understood in terms of an off-lattice model with 5-6 atoms per amino acid and a minimalistic potential, in which folding is driven by backbone hydrogen bonding and effective hydrophobic attraction. |
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Keywords: | protein folding folding thermodynamics folding kinetics three‐helix bundle unstructured protein Monte Carlo simulation |
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