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Proteins are macromolecules that consist of linear-bonded amino acids. They are essential elements in various metabolic processes. The three-dimensional structure of a protein is determined by the order of amino acids, also referred to as the protein sequence. This conformation corresponds to the structural state in which the protein is functionally active. However, relationships between protein sequence, structure and function have not been fully understood yet. Additionally, information about structural properties or even the entire protein structure are crucial for understanding the dynamics that define protein functionality and mechanisms. From this, the role of a protein in its molecular context can be described closely. For instance, interactions can be investigated and comprehended as a biological dynamic network that is sensitive to alternations, i.e. changes which are caused by diseases. Such knowledge can aid in drug design, whereas compounds need to be specifically tailored and adjusted to their molecular targets. Protein energy profile-basedmethods can be applied to investigate protein structures concerning dynamics and alternations. The publications enclosed to this work discuss in general the scientific potentials of energy profilebased techniques and algorithms. On the one hand, changes in stability caused by protein mutations and proteinligand interactions are discussed in the context of energy profiles. On the other hand, energetic relations to protein sequence, structure and function are elucidated in detail. Finally, the presented discussions focus on recent enhancements of the eProS (energy profile suite) database and toolbox. eProS freely provides all elucidated methodologies to the scientific community. Thus, one can address biological questions with the presented methods at hand. Additionally, eProS provides annotations related to foreign databases. This ensures a broad view on biological data and information. In particular, energetic characteristics can be identified which contribute to a protein’s structure and function.
The bachelor thesis is about cis-trans isomerization of Xaa-Pro (Xaa = any amino acid), their quantitative acquisition and the selection of 3D structure information for the prediction with a support vector machine (SVM). The quantitative detection of occurrence of cis-, trans- and cis/trans conformation in membrane proteins will be examined and evaluated. The 3D structure informa-tions include 12 features, the amino acids around proline and are including of proline. These include the inside/outside classification, the real secondary structure, energy consideration, as well as five further amino acid occur properties within a defined radius of the proline. From this information, a data set was created for the SVM. This program is used for the prediction of unknown and known Xaa Pro Isomerisms. The methods for the analysis were implemented with the platform independent programming language Java. Two programs have emerged from the work to a Xaa PIPT for the quantitative detection and extracting structural information and m Xaa-PIPT to the pure prediction of Xaa-Pro isomerism in protein structures. 389 Membrane proteins from the PDB (Protein Data Bank) served as a basis. The data were also statistically analysed and evaluated.