Sweet proteins offer a natural route to cutting added sugar. Monellin is a protein that is 90,000 times sweeter than sucrose but has limited use due to poor heat and pH stability. Our project aims to modify MNEI, a single-chain engineered variant of monellin, to create a thermostable sweetener that is applicable in real-world situations. An in silico protein design pipeline was developed for systematic design of Thermostable MNEI Variants. In brief, an exhaustive Rosetta point mutation scan was performed to assess all possible single and double mutations of MNEI. The resulting ΔΔG values were then used to rank mutations by predicting the folding free energy to evaluate stability. Subsequently, Molecular Dynamics were then performed to evaluate the conformational stability of MNEI and its variants. The most stable variants were then cloned into pET-28a(+) and expressed in E. coli NiCo21(DE3) for future experimental validations.