FoldIndex(C): a simple tool to predict whether a given protein sequence is intrinsically unfolded
Top Cited Papers
- 14 June 2005
- journal article
- Published by Oxford University Press (OUP) in Bioinformatics
- Vol. 21 (16) , 3435-3438
- https://doi.org/10.1093/bioinformatics/bti537
Abstract
An easy-to-use, versatile and freely available graphic web server, FoldIndex is described: it predicts if a given protein sequence is intrinsically unfolded implementing the algorithm of Uversky and co-workers, which is based on the average residue hydrophobicity and net charge of the sequence. FoldIndex has an error rate comparable to that of more sophisticated fold prediction methods. Sliding windows permit identification of large regions within a protein that possess folding propensities different from those of the whole protein.Keywords
This publication has 16 references indexed in Scilit:
- Evolution of clams (cholinesterase-like adhesion molecules): structure and function during developmentFrontiers in Bioscience-Landmark, 2005
- Protein Disorder PredictionStructure, 2003
- Natively unfolded C‐terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulinProteins-Structure Function and Bioinformatics, 2003
- GlobPlot: exploring protein sequences for globularity and disorderNucleic Acids Research, 2003
- NORSp: predictions of long regions without regular secondary structureNucleic Acids Research, 2003
- p53 Contains Large Unstructured Regions in its Native StateJournal of Molecular Biology, 2002
- Intrinsic Disorder and Protein FunctionBiochemistry, 2002
- Removing near-neighbour redundancy from large protein sequence collections.Bioinformatics, 1998
- Refined Three-Dimensional Structure of Cat-Muscle (M1) Pyruvate Kinase at a Resolution of 2.6 ÅActa Crystallographica Section D-Biological Crystallography, 1996
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982