TRAMPLE
TRAMPLE predicts and annotates transmembrane protein sequences, including alpha-helical and beta-strand (beta-barrel) segments, signal peptides, secondary structure, and membrane topology to support membrane protein characterization.
Key Features:
- Transmembrane Segment Prediction: Predicts both alpha-helical and beta-strand transmembrane segments.
- Neural Network with Evolutionary Profiles: Applies neural network-based methodologies that leverage evolutionary profiles as input to improve prediction accuracy.
- Signal Peptide Detection: Detects signal peptides for subcellular targeting.
- Secondary Structure Prediction: Predicts secondary structure elements to inform folding and functional inference.
- Topology Determination: Predicts orientation and topology of transmembrane helices (HTMs), including analysis of positively charged residues that are more abundant in extra-cytoplasmic regions.
- Model Optimization and Accuracy: Employs dynamic programming-like algorithms to optimize predictions and reports up to 78% residue accuracy for beta-strand topography when evolutionary information is used.
- HMM Integration: Integrates hidden Markov models (HMM) with neural network approaches for topology prediction.
- Validation: Validated using cross-validation and double-blind test sets.
Scientific Applications:
- Membrane Protein Annotation: Supports annotation of membrane protein topology and secondary structure, including cases lacking homologous sequences in existing databases.
- Proteome Analysis: Enables proteome-wide identification and characterization of outer membrane proteins, including beta-barrel structures.
- Integral Membrane Protein Research: Facilitates studies of orientation, location, function, and interactions of integral membrane proteins.
Methodology:
Integrates neural network-based approaches with hidden Markov models (HMM), uses evolutionary profiles/information as input, optimizes predictions via dynamic programming-like algorithms, and validates performance by cross-validation and double-blind test sets.
Topics
Details
- Tool Type:
- web application
- Operating Systems:
- Linux, Windows, Mac
- Programming Languages:
- JavaScript
- Added:
- 2/10/2017
- Last Updated:
- 11/25/2024
Operations
Publications
Fariselli P, Casadio R. HTP: a neural network-based method for predicting the topology of helical transmembrane domains in proteins. Bioinformatics. 1996;12(1):41-48. doi:10.1093/bioinformatics/12.1.41. PMID:8670618.
Martelli PL, Fariselli P, Krogh A, Casadio R. A sequence-profile-based HMM for predicting and discriminating β barrel membrane proteins. Bioinformatics. 2002;18(suppl_1):S46-S53. doi:10.1093/bioinformatics/18.suppl_1.s46. PMID:12169530.
Rost B, Fariselli P, Casadio R. Topology prediction for helical transmembrane proteins at 86% accuracy–Topology prediction at 86% accuracy. Protein Science. 1996;5(8):1704-1718. doi:10.1002/pro.5560050824. PMID:8844859. PMCID:PMC2143485.
Jacoboni I, Martelli PL, Fariselli P, De Pinto V, Casadio R. Prediction of the transmembrane regions of β‐barrel membrane proteins with a neural network‐based predictor. Protein Science. 2001;10(4):779-787. doi:10.1110/ps.37201. PMID:11274469. PMCID:PMC2373968.
Fariselli P, Finelli M, Rossi I, Amico M, Zauli A, Martelli PL, Casadio R. TRAMPLE: the transmembrane protein labelling environment. Nucleic Acids Research. 2005;33(Web Server):W198-W201. doi:10.1093/nar/gki440. PMID:15980454. PMCID:PMC1160201.