CCHMM_PROF: a HMM-based coiled-coil predictor with evolutionary information
نویسندگان
چکیده
MOTIVATION The widespread coiled-coil structural motif in proteins is known to mediate a variety of biological interactions. Recognizing a coiled-coil containing sequence and locating its coiled-coil domains are key steps towards the determination of the protein structure and function. Different tools are available for predicting coiled-coil domains in protein sequences, including those based on position-specific score matrices and machine learning methods. RESULTS In this article, we introduce a hidden Markov model (CCHMM_PROF) that exploits the information contained in multiple sequence alignments (profiles) to predict coiled-coil regions. The new method discriminates coiled-coil sequences with an accuracy of 97% and achieves a true positive rate of 79% with only 1% of false positives. Furthermore, when predicting the location of coiled-coil segments in protein sequences, the method reaches an accuracy of 80% at the residue level and a best per-segment and per-protein efficiency of 81% and 80%, respectively. The results indicate that CCHMM_PROF outperforms all the existing tools and can be adopted for large-scale genome annotation. AVAILABILITY The dataset is available at http://www.biocomp.unibo.it/ approximately lisa/coiled-coils. The predictor is freely available at http://gpcr.biocomp.unibo.it/cgi/predictors/cchmmprof/pred_cchmmprof.cgi. CONTACT [email protected].
منابع مشابه
Evolutionary Patterns in Coiled-Coils
Models of protein evolution are used to describe evolutionary processes, for phylogenetic analyses and homology detection. Widely used general models of protein evolution are biased toward globular domains and lack resolution to describe evolutionary processes for other protein types. As three-dimensional structure is a major constraint to protein evolution, specific models have been proposed f...
متن کاملSCORER 2.0: an algorithm for distinguishing parallel dimeric and trimeric coiled-coil sequences
MOTIVATION The coiled coil is a ubiquitous α-helical protein structure domain that directs and facilitates protein-protein interactions in a wide variety of biological processes. At the protein-sequence level, coiled coils are quite straightforward and readily recognized via the conspicuous heptad repeats of hydrophobic and polar residues. However, structurally they are more complicated, existi...
متن کاملCC+: a relational database of coiled-coil structures
UNLABELLED We introduce the CC+ DATABASE, a detailed, searchable repository of coiled-coil assignments, which is freely available at http://coiledcoils.chm.bris.ac.uk/ccplus. Coiled coils were identified using the program SOCKET, which locates coiled coils based on knobs-into-holes packing of side chains between alpha-helices. A method for determining the overall sequence identity of coiled-coi...
متن کاملAnalysis of variance of nanofluid heat transfer data for forced convection in horizontal spirally coiled tubes
In the present study, an experimental study is carried out to investigate the effect of adding Al and Cu nanoparticles to the base fluid (water) on the heat transfer rate in a spirally coiled tube. The spirally coiled tube is fabricated from the straight copper tube with the inner and outer coil diameters of 100 and 420 mm, respectively. The experiments have been done for water and two types of...
متن کاملStructures of smooth muscle myosin and heavy meromyosin in the folded, shutdown state.
Remodelling the contractile apparatus within smooth muscle cells allows effective contractile activity over a wide range of cell lengths. Thick filaments may be redistributed via depolymerisation into inactive myosin monomers that have been detected in vitro, in which the long tail has a folded conformation. Using negative stain electron microscopy of individual folded myosin molecules from tur...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Bioinformatics
دوره 25 21 شماره
صفحات -
تاریخ انتشار 2009