Prediction of Residue-specific Contributions to Binding and Thermal Stability Using Yeast Surface Display.

ABSTRACT: Accurate prediction of residue burial as well as quantitative prediction of residue-specific contributions to protein stability and activity is challenging, especially in the absence of experimental structural information. This is important for prediction and understanding of disease causing mutations, and for protein stabilization and design. Using yeast surface display of a saturation mutagenesis library of the bacterial toxin CcdB, we probe the relationship between ligand binding and expression level of displayed protein, with in vivo solubility in E. coli and in vitro thermal stability. We find that both the stability and solubility correlate well with the total amount of active protein on the yeast cell surface but not with total amount of expressed protein. We co

SUBMITTER: Ahmed S 

PROVIDER: S-EPMC8814602 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature