Protein disorder prediction: implications for structural proteomics
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Protein disorder prediction : implications for structural proteomics. / Linding, Rune; Jensen, Lars Juhl; Diella, Francesca; Bork, Peer; Gibson, Toby J; Russell, Robert B.
In: Structure, Vol. 11, No. 11, 2003, p. 1453-9.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Protein disorder prediction
T2 - implications for structural proteomics
AU - Linding, Rune
AU - Jensen, Lars Juhl
AU - Diella, Francesca
AU - Bork, Peer
AU - Gibson, Toby J
AU - Russell, Robert B
PY - 2003
Y1 - 2003
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.
AB - 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.
M3 - Journal article
C2 - 14604535
VL - 11
SP - 1453
EP - 1459
JO - Structure
JF - Structure
SN - 0969-2126
IS - 11
ER -
ID: 40740729