Protein Engineering by Chemical and Genetic MethodsApplications to Protein Recognition and Thrombin Function

TL;DRAbstract

In the past three decades, the advent of recombinant DNA technology allowed the site-specific alteration of a given polypeptide chain at a glance, thus much expanding the tools available to study the molecular mechanisms of protein folding, stability, and function. This approach, also known as protein engineering, is based on the possibility of modifying the chemical composition of a protein at a single or multiple sites with the 20 available coded amino acids, thus obtaining recombinant mutant proteins with altered structure, function, or stability properties. Evaluation of the effects of the mutation on the property under investigation (e.g., folding, stability or molecular recognition) will allow quantitative estimation of the contribution of that specific amino acid which has been mutated in the wild-type protein. This information will in turn help in understanding the physico-chemical determinants exploited by natural polypeptide chains to spontaneously acquire a unique, stable an

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