The discovery of the human genome was a milestone in the study of genetics, especially in the area of proteins. The human genome provides unique working tool, providing the opportunity of coming across new proteins and therefore obtaining information about the biological processes that take place within each cell. Proteins are one of the most important chemical compounds of living beings because they participate in most of the functions necessary for life. One of the most important topics within the proteins? research is the study and collection of protein structures and the possible movements this structures can carry out.

Few years ago a new approach has made its way in the proteins field. This new approach, which could be designated as Biokinematics, tries to apply techniques and concepts of robotics and kinematics to the study of proteins. Tecniques like Probabilistic Roadmap mapping, modal analysis or rigidity analysis have been applied in order to obtain protein motion paths.

The aim of this project is to simulate protein function movement using proteins? real degrees of freedom.  A procedure is being developed that performs a sequential and incremental rotation of the dihedral angles until they reach their final value. To determine the angular increment for each of the degrees of freedom durign the sumulation process, the algorithm evaluates the potential energy of the protein (potential field of AMBER parameters Cornell) along the simulation, but avoid using minimization procedures. In order to increase the quality of the experimental data positions, an algorithm has been developed for the normalization of the protein structure. Currently, the algorithm is able to correct errors regarding peptide planes and interatomic bond lengths. The results are promising obtaining a more stable protein (the potential energy is about 15% lower in the normalized structure) maintaining the biological sense. Every algorithm is implemented in a software under development called GIMPRO.