Protein-ligand interactions advantages

This kind of shift mapping has been used extensively in NMR studies of protein-ligand interactions. Shuker et al.1/2 used this method to advantage in a lead generation approach that effectively covalently links two... 

So far there have been relatively few applications of electrophoresis at elevated hydrostatic pressures. However, this method has several advantages over other methods such as optical methods it is a simple and direct means of studying dissociation and denaturation processes, and of describing the thermodynamics of protein-ligand interactions. These qualitative and quantitative studies can be performed using small amounts of pure proteins or complex protein mixtures. In addition, this technique permits separation and subsequent isolation of the different protein conformational states or subunits. 

The yeast two-hybrid system detects protein-protein or protein-peptide interactions in vivo. The target or bait protein and the ligand library are fused to either the DNA-binding domain or the transcription activation domain. Yeast cells are transformed with both plasmids and only the transformants expressing the protein-ligand interaction are selected (Y2). The main advantage is the one-step in vivo screening however, the library size is limited to about lO because of the transformation efficiency of the cells. 

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