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:
prediction of
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