Team:Duke/Basic Part
Basic Parts
Thermostability of GRFT
In order to improve the stability of the monomeric (3LL2) and homodimeric (2HYQ) griffithsin proteins, we used the amino sequence found on the protein data bank and mutated residues that contributed to structure destabilization. Using the YASARA and ZDOCK modeling packages, we were able to identify residues with high B factors and predict which amino acid changes were required to improve the stability of folded structure. After changing these amino acids, we simulated the interactions and binding interfaces between our thermoengineered proteins and antibodies and glycoproteins. Through this, we determined that our thermostable variants were predicted to have higher melting temperatures and have preserved binding loops. Please check out our modeling page for more information on the process of thermoengineering! (LINK HERE)
Because of the engineering and significance of this part, the part numbered BBa_K2464004 is the best part we added to the registry this year. All of the other parts we submitted to the registry are basic parts. Click here for our comprehensive list.
