@phdthesis{Bittrich2014,
  type      = {Master Thesis},
  author    = {Sebastian Bittrich},
  title     = {Toward a Unified Assessment Protocol for Local and Global Protein Structure Stability and Quality Using Knowledge-Based Potentials},
  url       = {https://nbn-resolving.org/urn:nbn:de:bsz:mit1-opus4-63097},
  year      = {2014},
  abstract  = {Proteins are involved in almost every aspect of life, mediating a wide range of cellular tasks. The protein sequence dictates the spatial arrangement of the residues and thus ultimately the function of a rotein. Huge effort is put into cumbersome structure eludication experiments which obtain models describing the observed spatial conformation of a protein, enabling users to predict their function, to understand their mode of action or to design tailored drugs to cure disease caused by misfolded or misregulated proteins. However, the result of structure determination experiments are merely models of reality, made under simplifying assumptions - sometimes containing major undetected errors. On the other hand, such experiments are resource demanding and they cannot supply the actual demand. Thus, scientists are predicting the structure of proteins in silico, resulting in models that are even more prone to error. In consequence, the structure biologists search after a practicable definition of structure quality and over the last two decades several model quality assessment programs emerged, measuring the local and global quality of peculiar structures. Seven representatives were studied, regarding the paradigms they follow and the features they use to describe the quality of residues. Their predications were compared, showing that there is almost no common ground among the tools. Is there a way to combine their statements anyway? Finally, the accumulated knowledge was used to design a novel evaluation tool, addressing problems previously spotted. Thereby, high quality of its predication as well as superior usability was key. The strategy was compared to existing approaches and evaluated on suitable datasets.},
  language  = {en}
}