IMPORTANT: Please submit jobs with at least 3 second interval and do not submit more than 50 jobs at a time. Otherwise, the jobs will be deleted and your IP address blocked.
Proteins are dynamic and flexible macromolecules. Upon changes in the environment, the protein backbone can undergo significant ordered conformational changes and switch from one folded conformation to another. This web-server predicts residue positions that may be involved in such ordered conformational switches. The prediction can be performed using either a user-supplied protein sequence or a protein structure in a Protein Data Bank (PDB) file. If a protein sequence is submitted, then the prediction is performed using sequence-derived information only (such as the profile of evolutionary conservation of residue positions). If a PDB file is submitted, then the prediction is performed using sequence-derived information and solvent accessibility of residue positions calculated from this file. Please note that this web-server is not meant to predict protein disorder (you may refer to DisProt for a list of disorder predictors). For more information on the methodology and accuracy of the prediction please refer to the original publication (Kuznetsov, 2008) and help link.
Web-server citation: I.B.Kuznetsov and M.McDuffie, 2008, FlexPred: a web-server for predicting residue positions involved
in conformational switches in proteins. Bioinformation, 3(3):134-136
Methodology citation: I.B.Kuznetsov, 2008, Ordered conformational change in the protein backbone:
conformationally variable positions from sequence and low-resolution structural data.
Proteins: Structure, Function and Bioinformatics, 72(1):74-87
Please address your questions and comments to Igor Kuznetsov