Publisher's Synopsis
Encyclopaedia of Protein Engineering: Applications In Science, Medicine And Industr presents in-depth discus- sions of various methods for protein engineering featuring contributions from renowned experts from different counties. It covers significant aspects of methods and applications in the design of novel proteins with different functions. Rational design in other words computational design of proteins requires the amino acid sequence, 3D structure and function knowledge of the protein of interest. This method provides controllable amino acid sequence changes (insertion, deletion or substitution). Controlled changes are important to determine the effect of individual residue changes on the protein structure, folding, stability or function. Knowledge of three-dimensional structure is a key for understanding the biological function. Although understanding of 3D structure of proteins is crucial in terms of their function, only about 1 % of proteins for which the amino acid sequence is known, had their 3D structure determined because of the time consuming nature and difficulty of crystallographic experimental methods. As a result, the gap between the numbers of known sequences and structures continuously grows. In addition to enlarging databases, improvements in sequence comparison, fold recognition and protein modelling algorithms have supported the enhance- ment of protein structure prediction studies based on computer modelling methods to bridge this gap. Encyclopaedia of Protein Engineering: Applications In Science, Medicine And Industr presents in-depth discus- sions of various methods for protein engineering featuring contributions from renowned experts from different counties. It covers significant aspects of methods and applications in the design of novel proteins with different functions. Rational design in other words computational design of proteins requires the amino acid sequence, 3D structure and function knowledge of the protein of interest. This method provides controllable amino acid sequence changes (insertion, deletion or substitution). Controlled changes are important to determine the effect of individual residue changes on the protein structure, folding, stability or function. Knowledge of three-dimensional structure is a key for understanding the biological function. Although understanding of 3D structure of proteins is crucial in terms of their function, only about 1 % of proteins for which the amino acid sequence is known, had their 3D structure determined because of the time consuming nature and difficulty of crystallographic experimental methods. As a result, the gap between the numbers of known sequences and structures continuously grows. In addition to enlarging databases, improvements in sequence comparison, fold recognition and protein modelling algorithms have supported the enhance- ment of protein structure prediction studies based on computer modelling methods to bridge this gap.
