https://www.selleckchem.com/pr....oducts/ly2157299.htm
These findings reveal how MD can predict how changes in the "second shell" residues around substrate binding sites influence affinity in simple protein structures. Our results reveal why seemingly identical ε subunits in different ATP synthases have radically different ATP binding affinities. This study may lead to greater utility of molecular dynamics as a tool for protein design and exploration of protein design and function. This study may lead to greater utility of molecular dynamics as a tool for protein design and exploration of
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