| 초록 |
The quest for protein stability improvement is still on for a wide range of industrial applications which could be more convenient and economically feasible. Introduction of stabilizing mutations for a desired purpose by rational engineering has been successfully reported. However, the specificity of protein structure, function and stability hampers the design of generalized protein engineering methods towards stability. In this study, an attempt to enhance the protein stability by utilizing the advantageous property of arginine over lysine which has similar physicochemical property was reported. With green fluorescent protein as a model system, a fluorescent variant was created by mutating the maximum possible number of lysine residues on the surface to arginine while retaining the structure and function. |
