István Simon

TL;DR: The IUPred server presents a novel algorithm for predicting such regions from amino acid sequences by estimating their total pairwise interresidue interaction energy, based on the assumption that IUP sequences do not fold due to their inability to form sufficient stabilizing inter Residue interactions.

TL;DR: The user is allowed to submit additional information about segment localization to enhance the prediction power, which improves the prediction accuracy as well as helps the interpretation of experimental results, i.e. in epitope insertion experiments.

TL;DR: The method successfully predicted all the transmembrane segments in 143 proteins out of the 158, and for 135 of these proteins both the membrane spanning regions and the topologies were predicted correctly.

TL;DR: This so-called dense alignment surface (DAS) method is shown to perform on par with earlier methods that require extra information in the form of multiple sequence alignments or the distribution of positively charged residues outside the transmembrane segments, and thus improves prediction abilities when only single-sequence information is available.

TL;DR: IUPred, a novel method for estimating the total pairwise interaction energy of proteins of known structure, based on a quadratic form in the amino acid composition of the protein, is presented and substantiates the concept of protein disorder.