ArticleThe journal of physical chemistry letters2025
Density Functional Theory Calculations to Investigate the Role Played by an Aspartate Dyad in Hsp60-Catalyzed ATP Hydrolysis.
Article in The journal of physical chemistry letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Adenosine 5'-triphosphate (ATP) hydrolysis is one of the most significant reactions in biochemistry. In chaperone proteins, energy released by hydrolysis enables them to carry out their function and help other proteins (called "clients") to fold into their functional form. Here, we run Density Functional Theory calculations on three cluster models of the Hsp60 active site extracted from our previous molecular dynamics simulations of the 14-meric Hsp60 double-ring complex: our aim is to qualitatively investigate the mechanisms of ATP hydrolysis in different scenarios where the chaperone closes a dyad composed of catalytic aspartates Asp50 and Asp397. Since dyad closure raises Asp p
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