Protein disorder prediction: implications for structural proteomics.

@article{Linding2003, 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.}, author = {Linding, Rune and Jensen, Lars J. and Diella, Francesca and Bork, Peer and Gibson, Toby J. and Russell, Robert B. }, citeulike-article-id = {2054445}, journal = {Structure}, keywords = {article-nar, article-predikin, circular, computer, conformation, crystallography, dichroism, domain, homology, ligand, magnetic, models, network, neural, protein, proteome, ray, resonance, sensitivity, specificity, spectroscopy, src, statistics, temperature, theoretical, topic, ultraviolet, x-ray}, month = {Nov}, number = {11}, pages = {1453--1459}, posted-at = {2007-12-04 03:22:13}, priority = {2}, title = {Protein disorder prediction: implications for structural proteomics.}, volume = {11}, year = {2003} }

TY - JOUR ID - Linding2003 L3 - citeulike-article-id:2054445 TI - Protein disorder prediction: implications for structural proteomics. JF - Structure VL - 11 IS - 11 SP - 1453 EP - 1459 N2 - 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. KW - article-nar KW - article-predikin KW - circular KW - computer KW - conformation KW - crystallography KW - dichroism KW - domain KW - homology KW - ligand KW - magnetic KW - models KW - network KW - neural KW - protein KW - proteome KW - ray KW - resonance KW - sensitivity KW - specificity KW - spectroscopy KW - src KW - statistics KW - temperature KW - theoretical KW - topic KW - ultraviolet KW - x-ray AU - Linding, Rune AU - Jensen, Lars AU - Diella, Francesca AU - Bork, Peer AU - Gibson, Toby AU - Russell, Robert PY - 2003/Nov// ER -