摘要

Structural comparison indicates that the loop region between 3 and 4 of SsArd1 is extended relative to the corresponding region in mesophilic Nats, and forms a plastic hydrogen-bond network mainly at two serine residues. Strikingly, two single-point mutants showed approximate to 3 degrees C decrease in melting temperature, and two other variants showed approximate to 7 degrees C decrease; this correlated with significantly reduced enzymatic activity. To our knowledge, this is the first discovery of a loop region capable of remarkably improving protein thermostability. This provides a novel route to engineer heat-resistant proteins.

  • 出版日期2016-2-2