A newly introduced salt bridge cluster improves structural and biophysical properties of de novo TIM barrels.

ABSTRACT: Protein stability can be fine-tuned by modifying different structural features such as hydrogen-bond networks, salt bridges, hydrophobic cores, or disulfide bridges. Among these, stabilization by salt bridges is a major challenge in protein design and engineering since their stabilizing effects show a high dependence on the structural environment in the protein, and therefore are difficult to predict and model. In this work, we explore the effects on structure and stability of an introduced salt bridge cluster in the context of three different de novo TIM barrels. The salt bridge variants exhibit similar thermostability in comparison with their parental designs but important differences in the conformational stability at 25°C can be observed such as a highly stabilizing effect for two of t

SUBMITTER: Kordes S 

PROVIDER: S-EPMC8820119 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature