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• W2092249511 startingPage "2054" @default.
• W2092249511 abstract "The mechanical unfolding of proteins under a stretching force has an important role in living systems and is a logical extension of the more general protein folding problem. Recent advances in experimental methodology have allowed the stretching of single molecules, thus rendering this process ripe for computational study. We use all-atom Monte Carlo simulation with a Gō-type potential to study the mechanical unfolding pathway of ubiquitin. A detailed, robust, well-defined pathway is found, confirming existing results in this vein though using a different model. Additionally, we identify the protein's fundamental stabilizing secondary structure interactions in the presence of a stretching force and show that this fundamental stabilizing role does not persist in the absence of mechanical stress. The apparent success of simulation methods in studying ubiquitin's mechanical unfolding pathway indicates their potential usefulness for future study of the stretching of other proteins and the relationship between protein structure and the response to mechanical deformation." @default.
• W2092249511 created "2016-06-24" @default.
• W2092249511 creator A5016231212 @default.
• W2092249511 creator A5082765817 @default.
• W2092249511 date "2007-03-01" @default.
• W2092249511 modified "2023-09-23" @default.
• W2092249511 title "The Mechanical Unfolding of Ubiquitin through All-Atom Monte Carlo Simulation with a Gō-Type Potential" @default.
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• W2092249511 doi "https://doi.org/10.1529/biophysj.106.081257" @default.
• W2092249511 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1861770" @default.
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• W2092249511 hasPublicationYear "2007" @default.
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