@phdthesis{Oswald2014,
  type      = {Master Thesis},
  author    = {Silvio Oswald},
  title     = {vestigations on quantilized energetically sub-profiles in Pfam families and discussion concerning their information content},
  url       = {https://nbn-resolving.org/urn:nbn:de:bsz:mit1-opus4-63083},
  year      = {2014},
  abstract  = {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.},
  language  = {en}
}