Protein disorder prediction: implications for structural proteomics.
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. We present here DisEMBL, 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. The tool is freely available via a web interface (http://dis.embl.de) and can be downloaded for use in large-scale studies.
Linding
Rune
R
EMBL, Biocomputing Unit, Meyerhofstr 1, D-69117 Heidelberg, Germany. linding@embl.de
Jensen
Lars Juhl
LJ
Diella
Francesca
F
Bork
Peer
P
Gibson
Toby J
TJ
Russell
Robert B
RB
D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D006801:Humans; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008962:Models, Theoretical; D016571:Neural Networks, Computer; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D020543:Proteome / Q000737:chemistry*; D012680:Sensitivity and Specificity; D013223:Statistics as Topic; D013696:Temperature; D014466:Ultraviolet Rays; D018909:src Homology Domains
D008024:Ligands; D011506:Proteins; D020543:Proteome