Protein structures are essential elements in every biological system evolved on earth, where they function as stabilizing elements, signaltransducers or replication machin eries. They are consisting of linear-bonded amino acids, which determine the three-dimensional structure of the protein, whereas the structure in turn determines the function. The native and biological active structure ofa protein can be understood as the folding state of a polypeptide chain at the global minimum of free energy.
By means of protein energy profiling, which is an approach derived from statistical physics it is possible to assign a so called energy profile to a protein structure. Such an energy profile describes the local energetic interaction features of every amino acid within the structure and introduces an energetic point of view, instead of a structural or sequential onto proteins.
This work aims to give a perspective to the question of how we may gain pattern information out of energy profiles. The concrete subjects are energy-mapped Pfam family alignments and investigations on finding motifs or patterns indiscretizised energy profile segments.
In der vorliegenden Arbeit werden strukturelle und funktionelle Proteinmotive hinsichtlich ihrer energetischen Charakteristika untersucht und nach energetischen Abständen über hierarchische Clusterverfahren geclustert. Dabei sollen Gesetzmäßigkeiten offen gelegt werden, die sich über die Abstraktionsebenen der Sequenz, Struktur, Funktion und der Energie erstrecken.