RFPR-IDP: reduce the false positive rates for intrinsically disordered protein and region prediction by incorporating both fully ordered proteins and disordered proteins.
Yumeng LiuXiaolong WangBin LiuPublished in: Briefings Bioinform. (2021)
Keyphrases
- amino acids
- disordered regions
- protein sequences
- amino acid sequences
- intrinsically disordered
- protein function
- subcellular localization
- protein structure
- experimentally determined
- contact map
- protein structure prediction
- contact maps
- protein secondary structure
- predicting protein
- secondary structure
- false positive rate
- physicochemical properties
- protein protein interactions
- protein chains
- protein interaction
- molecular biology
- drug design
- computational biology
- protein secondary structure prediction
- protein function prediction
- protein classification
- protein interaction data
- protein protein
- gene ontology
- sequence alignment
- false positives
- coarse grained
- detection rate
- multiple sequence alignments
- protein protein interaction networks
- protein folding
- mass spectrometry
- graph theory
- sequence analysis
- protein complexes
- computational approaches
- functional modules