Combining conservation and rigidity methods to detect critical residues in proteins

The structure and the functionality of proteins are closely related to each other. Therefore, analyzing the structural and dynamical properties of proteins is crucial for understanding their role in the basic biology of organisms. Some specific regions in the protein may play a critical role in its structural, dynamical and functional properties. For example, proteins usually bind through a specific site on their surfaces which tends to be highly conserved. Proteins also have flexible regions such as hinges, which allow them to undergo small or large scale domain motions. Finding these critical regions can facilitate the analysis of protein flexibility and improve the performance of docking algorithms. Here we combine the properties of two different analysis methods - conservation through evolutionary traces and rigidity analysis, to estimate the relative importance of amino acids in proteins.