Computational Model of Synthetic Construct of Monellin-A Chain

Most proteins are tasteless and flavorless, while some proteins elicit a sweettaste response on the human palate. Six proteins, thaumatin, monellin, mabinlin, brazzein, egg lysozyme, and neoculin (previously considered as curculin) have been identified as sweet-tasting proteins. Information on the structure-sweetness relationship for these proteins would help not only in the clarification of the mechanism of interaction of sweet-tasting proteins with their receptors, but also in the design of more effective low-calorie sweeteners. We have modeled the three dimensional structure of monellin synthetic construct using swiss model server and studied the conformation of the secondary structure using Ramachandran plot statistics. It is observed that the structure coincides with its berry counterpart 1MOL_B chain and, the rmsd distance of is 1.61 A is observed. The structure is deposited at the protein databank and id is 2GPK.