Protein structure prediction and folding dynamics

For most proteins known today their three-dimensional structure is crucial in determining biological function. As experimental determination of protein structure is difficult and costly compared to relatively simple and cheap sequencing, it is of great practical interest to predict a protein's structure from a given amino acid sequence. Another question in the study of protein structure is how the protein folds into its biologically active (native) state overcoming free energy barriers and visiting possible intermediate states. As protein misfolding is associated with several diseases, this is of bio-medical importance, too. Moreover, folding dynamics are of fundamental interest as a mesoscopic system displaying cooperative effects. In this talk I shall attempt to give a short introduction to these two aspects of protein folding and present some results from my PhD thesis. There, so-called structural profiles were used which may act as a link between protein sequence and structure for the task of structure prediction. In protein folding dynamics they may be used to define a potential leading towards the native state.