Quick SearchSelect Databanks to SearchCreate your QueryUse Analysis ToolsManage your Query ResultsManage your ProjectsCreate Custom ViewsDataBanks Information Page  
Name

TMAP

Search
Status The current release has 0 entries and was indexed 21-Sep-2004.
Creation date Completed 17th June 1999.
Description TMAP application details page

Displays membrane spanning regions

This program predicts transmembrane segments in proteins, utilising the algorithm described in: "Persson, B. & Argos, P. (1994) Prediction of transmembrane segments in proteins utilising multiple sequence alignments J. Mol. Biol. 237, 182-192."

tmap reads in one or more aligned protein sequences.

Two sets of propensity values are then used for the calculations: onefor the middle, hydrophobic portion and one for the terminal regions ofthe transmembrane sequence spans. Average propensity values arecalculated for each position along the alignment, with the contributionfrom each sequence weighted according to its dissimilarity relative tothe other aligned sequences.

Eight-residue segments are considered as potential cores oftransmembrane segments and elongated if thier middle propensity valuesare above a threshold. End propensity values are also considered asstop signals. Only helices with a length of 15 to 29 residues areallowed and corrections for strictly conserved charged residues aremade.

The method is more successful than predictions based upon singlesequences alone.

The results are plotted on a graph and written to a text file.

Literature "Persson, B. & Argos, P. (1994) Prediction of transmembrane segments in proteins utilsing multiple sequence alignments J. Mol. Biol. 237, 182-192."
WWW www.hgmp.mrc.ac.uk/Software/EMBOSS/Apps/tmap.html
Ftp The latest version of the EMBOSS package is available on ftp://ftp.uk.embnet.org/pub/EMBOSS/
Contact Original program by Bengt Persson and Patrick Argos.

This application was modified for inclusion in EMBOSS by Ian Longden (il@sanger.ac.uk) InformaticsDivision, The Sanger Centre, Wellcome Trust Genome Campus, Hinxton,Cambridge, CB10 1SA, UK.

See also
GARNIER Predicts protein secondary structure
HELIXTURNHELIX Report nucleic acid binding motifs
HMOMENT Hydrophobic moment calculation
PEPCOIL Predicts coiled coil regions
PEPNET Displays proteins as a helical net
PEPWHEEL Shows protein sequences as helices
Data-fields in SRS
Field Name
Short Name
Type
No. of Keys
No. of Entry References
Indexing Date
Status
ID id id 0 0   not indexed
JobName jnm index 0 0   not indexed
Loaders
EMBOSSDNASIMPLESEQ
EMBOSSPROTSIMPLESEQ
RFEMBOSSLOAD
SRS Description Structure ( srsgen.i , srsdb.i , href.i )
Syntax
Information
SRS Release 7.1.3    Copyright © 1997-2003 LION bioscience AG. All Rights Reserved. Terms of Use Feedback