A great challenge in the proteomics and structural genomics era is to predict protein structure and function, including identification of those proteins that are partially or wholly unstructured. Disordered regions in proteins often contain short linear peptide motifs (e.g. SH3-ligands and targeting signals) that are important for protein function. Linear peptide sites are catalogued by ELM.
DisEMBL is a computational tool for prediction of disordered/unstructured regions within a protein sequence. As no clear definition of disorder exists, we have developed parameters based on several alternative definitions, and introduced a new one based on the concept of ``hot loops'', i.e. coils with high temperature factors.
Avoiding potentially disordered segments in protein expression constructs can increase expression, foldability and stability of the expressed protein. DisEMBL is thus useful for target selection and the design of constructs as needed for many biochemical studies, particularly structural biology and structural genomics projects.
If you need further help please contact Rune Linding.