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Our aim in this review is to demonstrate the usefulness of the alanine scanning method in protein engineering, particularly in obtaining information on the effect of single-residue substitution on the conformational stability and dynamics of globular proteins. Firstly, we describe the experimental design of an alanine scanning library based on the intrinsic distribution of amino acid residues in a protein. The method described has been optimized with different statistical analysis and selection methods for the selection of the most appropriate alanine in position X of a target protein. The library screening is performed on the basis of the intrinsic rate of unfolding of the protein in which the alanine is substituted, its resistance to chemical denaturants and the capacity to discriminate among the different test proteins. The structural information obtained in this way is useful in predicting the physiological role of the protein and in the selection of novel biomaterials. In conclusion, we demonstrate the application of the alanine scanning method to the structure-stability relationship of the the major antibiotic binding pocket of penicillin binding protein 4 (PBP4). Our results indicate that D76 of the beta-