Stabilization of Multimeric Proteins via Intersubunit Cyclization.

ABSTRACT: Proteins with high catalytic efficiency and selectivity under mild conditions have long been appreciated by industrial and medicinal fields. These proteins, which are commonly multimeric, often possess low stability, impeding wider application. Currently, strategies to improve the stability of multimeric proteins concentrate on enhancing the interaction at internal interface of the subunits. In this report, we confirmed that the largely underestimated subunit terminal ends are as significant as the internal interface for protein stability. By connecting both the terminal ends and internal interface of subunits, the tetrameric Leifsonia alcohol dehydrogenase (LnADH) protein can been cyclized into a rigid form with significantly improved thermostability and resilience. The impr

SUBMITTER: Zhu L 

PROVIDER: S-EPMC5583479 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature