  We present a novel method that predicts transmembrane domains in proteins
using solely information contained in the sequence itself. The PRED-TMR
algorithm described, refines a standard hydrophobicity analysis with a
detection of potential termini ('edges', starts and ends) of transmembrane
regions. This allows one both to discard highly hydrophobic regions not
delimited by clear start and end configurations and to confirm putative
transmembrane segments not distinguishable by their hydrophobic composition.
The accuracy obtained on a test set of 101 non-homologous transmembrane
proteins with reliable topologies compares well with that of other popular
existing methods. Only a slight decrease in prediction accuracy was observed
when the algorithm was applied to all transmembrane proteins of the SwissProt
database (release 35). A WWW server running the PRED-TMR algorithm is available
at http://o2.db.uoa. gr/PRED-TMR/
