Protein purification and stability

This paper describes an improved bioprocess for producing Q-Griffithsin, a clinical-stage antiviral, using integrated autolysis, DNA hydrolysis, and precipitation to achieve high purity and yield without conventional chromatography.

The paper introduces Aggrescan3D, a tool for designing protein variants with improved solubility and reduced aggregation using 3D structures, and demonstrates its application on therapeutic proteins.

This paper describes a reliable method for purifying His-tagged and untagged E. coli Prs protein with high yield, purity, and activity.

The paper develops a computational model to analyze pH-stability of antibodies and applies it to proteases, identifying design principles for acid-stable proteins.

The paper develops a web server to predict protein surface polarity and pH/ionic strength dependence, showing antibody-antigen interfaces are as polar as Fab surfaces.