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Protein disorder prediction: Implications for structural proteomics

Item Type:Article
Title:Protein disorder prediction: Implications for structural proteomics
Creators Name:Linding, R. and Jensen, L.J. and Diella, F. and Bork, P. and Gibson, T.J. and Russell, R.B.
Abstract: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.
Keywords:Circular Dichroism, X-Ray Crystallography, Ligands, Magnetic Resonance Spectroscopy, Theoretical Models, Neural Networks (Computer), Protein Conformation, Proteins, Proteome, Sensitivity and Specificity, Statistics as Topic, Temperature, Ultraviolet Rays, src Homology Domains
Source:Structure with Folding & Design
Publisher:Cell Press
Page Range:1453-1459
Date:1 November 2003
Official Publication:https://doi.org/10.1016/j.str.2003.10.002
PubMed:View item in PubMed

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