Objective: To construct a phage-displayed site-directed random mutation combinatorial library of immunoglobμLin-binding molecμLes, which can provide reference the study of the in vitro molecμLar evolution of the library with different immunoglobμLins,and the relationship of their structure and function.

Many research groups successfully rely on whole-gene random mutagenesis and recombination approaches for the directed evolution of enzymes.

In vitro molecular directed evolution of enzymeis a new strategy in the engineering of novel biocatalysts, which mainly mimics the process of natural evolution to generaterandom mutation in the genes coding for useful enzymes by the techniques of error-prone PCR, and then in vitro recombinespositive mutations through various methods such .

Several receptor binding sites of LT were mutated randomly, then the R46,S106,L130 combined site-directed random mutation library and S106～F110 region random mutation library were displayed on a filamentous phage surface.

To construct the combined site_directed random mutation library of recombinant human Lymphotoxin (rhLT) for in vitro molecular evolution study, and to study the structure and function relationship.

Site-directed mutagenesis of functional gene fragment producing CTX-M-14-type extended-spectrum β-lactamase;

Study on site-directed mutagenesis and kinetics of trehalose synthase from Thermobifida fusca;

The Expression of hBmp-4 in the Pichia Pastoris and Its Site-Directed Mutagenesis;

Using recombinant glucagon expression system,the 21st aspartic acid was changed to be alanine by means of site directed mutagenesis.

Two p 16 mutants, P48L and D74N, were obtained by site directed mutagenesis using two step PCR method.

Human brain derived neurotrophic factor gene was used as template for oligonucleotide based site directed mutagenesis and PCR.