Affiliations: Institute of Medical Technology, University of
Tampere, Tampere, Finland | Tampere University Hospital, Tampere, Finland
Note: [] Corresponding author: Mauno Vihinen, Institute of Medical
Technology, University of Tampere, Tampere, FI-33014, Finland.
Fax: +358 33551 7710; E-mail: [email protected]
Abstract: In order to study protein function and activity structural data is
required. Since experimental structures are available for just a small fraction
of all known protein sequences, computational methods such as protein modelling
can provide useful information. Over the last few decades we have predicted,
with homology modelling methods, the structures for numerous proteins. In this
study we assess the structural quality and validity of the biological and
medical interpretations and predictions made based on the models. All the
models had correct scaffolding and were ranked at least as correct or good by
numerical evaluators even though the sequence identity with the template was as
low as 8%. The biological explanations made based on models were well in
line with experimental structures and other experimental studies. Retrospective
analysis of homology models indicates the power of protein modelling when made
carefully from sequence alignment to model building and refinement. Modelling
can be applied to studying and predicting different kinds of biological
phenomena and according to our results it can be done so with success.
Keywords: Protein models, homology modelling, missense mutations, biological predictions, evaluation, quality of protein models, disease-causing mutations, structural explanations for mutations
