Online Services of the Institute of Enzymology

BiSearch BiSearch is a primer-design algorithm for DNA sequences. It may be used for both bisulfite converted as well as for original not modified sequences. You can search various genomes with the designed primers to avoid non-specific PCR products.
DAS-TMfilter DAS-TMfilter predicts transmembrane segments by "Dense Alignment Surface" method (updated and modified version of the original DAS).
DNAbind DNAbind server predicts whether a protein is DNA-binding from its structure and/or sequence.
HMMTOP HMMTOP is an automatic prediction server for predicting topology and localization of transmembrane helices in transmembrane proteins.
IUPred Prediction of Intrinsically Unstructured Proteins. Intrinsically unstructured/disordered proteins have no single well-defined tertiary structure in their native, functional state. Our server recognizes such regions from the amino acid sequence based on the estimated pairwise energy content.
PDB_TM PDB_TM is the first comprehensive and up-to-date transmembrane protein selection of the Protein Data Bank (PDB).
SCPRED SCPRED can predict stabilization center residues in protein with unknown structure.
SCIDE SCIDE can identify the stabilization center residues in known protein structures.
SRide SRide can identify the stabilizing residues in proteins.
TMDET TMDET is an online tool for the detection of the transmembrane regions of membrane proteins by using their 3D structure only.
TOPDB The Topology Data Bank of Transmembrane Proteins (TOPDB) is currently the most complete and comprehensive collection of transmembrane protein datasets containing experimentally derived topology information.

Other prediction services
made in collaboration with
Institute of Enzymology

CYSREDOX Cysredox predicts the redox state of cysteins in proteins from multiple sequence alignments.
DAS DAS predicts transmembrane segments by "Dense Alignment Surface" method (original version).
PSORT-B PSORT-B is an updated method of PSORT family for prediction of localization in Gram-negative bacterial proteins.