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• W2158149487 abstract "Here, we study mechanical properties of eight 3-helix proteins (four right-handed and four left-handed ones), which are similar in size under stretching at a constant speed and at a constant force on the atomic level using molecular dynamics simulations. The analysis of 256 trajectories from molecular dynamics simulations with explicit water showed that the right-handed three-helix domains are more mechanically resistant than the left-handed domains. Such results are observed at different extension velocities studied (192 trajectories obtained at the following conditions: v = 0.1, 0.05, and 0.01 Å ps−1, T = 300 K) and under constant stretching force (64 trajectories, F = 800 pN, T = 300 K). We can explain this by the fact, at least in part, that the right-handed domains have a larger number of contacts per residue and the radius of cross section than the left-handed domains. Proteins 2014; 82:90–102. © 2013 Wiley Periodicals, Inc." @default.
• W2158149487 created "2016-06-24" @default.
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• W2158149487 date "2013-09-10" @default.
• W2158149487 modified "2023-10-16" @default.
• W2158149487 title "Right- and left-handed three-helix proteins. II. Similarity and differences in mechanical unfolding of proteins" @default.
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• W2158149487 doi "https://doi.org/10.1002/prot.24373" @default.
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• W2158149487 hasPublicationYear "2013" @default.
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