Conserved changes in secondary structure and aggregation properties of in vitro evolved proteins for thermo stability

Abstract

Most of the screening strategies of directed evolution involved in thermo stability deals with aggregation of proteins either directly or indirectly. Here in this work I investigated what happens in aggregation property and secondary structure of the protein when it improved its thermo stability by incorporating certain amino acid changes in the protein. To study these changes I picked randomly 12 different proteins and I analyzed their 25 different thermo stable mutants. I used open access online Software to get the aggregation propensity values and values for different secondary structure elements propensities of proteins. I compared the aggregation propensity and predicted secondary structure values of thermo stable mutants with their parent Wild type proteins. The stable mutants followed three different conserved patterns to improve their thermo stability.