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• W2966734375 abstract "Abstract In order to rationally design biopolymers that mimic biological functions, first, we need to elucidate the molecular mechanisms followed by nature. For example, the viral capsid is a macromolecular complex formed by self-assembled proteins which, in many cases, are biopolymers with an identical amino acid sequence. Specific protein-protein interactions drive the capsid self-assembly process, leading to several distinct protein interfaces. Following the hot-spot hypothesis, we propose a conservation-based methodology to identify those interface residues that are crucial elements on the self-assembly and thermodynamic stability of the capsid. We validate our predictions by computational free energy calculations using an atomic-scale molecular model of an icosahedral virus. Our results show that a single mutation in any of the hot-spots significantly perturbs the quaternary interaction, decreasing the absolute value of the binding free energy, without altering the tertiary structure. Our methodology can lead to a strategy to rationally modulate the capsid’s thermodynamic properties." @default.
• W2966734375 created "2019-08-13" @default.
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• W2966734375 date "2019-08-06" @default.
• W2966734375 modified "2023-09-27" @default.
• W2966734375 title "Hot-spots and their contribution to the self-assembly of the viral capsid: <i>in-silico</i> prediction and analysis" @default.
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• W2966734375 doi "https://doi.org/10.1101/723023" @default.
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