BiochemistrybioRxivPreprint
Structure and dynamics of a cold-active esterase reveals water entropy and active site accessibility as the likely drivers for cold-adaptation
N. Noby, H. Sabah Auhim, H. Worthy…·C. R. Pudney
This study determines the structure of a cold-active esterase and identifies increased substrate accessibility and water entropy tolerance as the main drivers of its cold adaptation.
DOI 10.1101/2021.02.23.432564