https://www.selleckchem.com/pr....oducts/filgotinib.ht
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 o
Me gusta
Comentario
Compartir
