2006
DOI: 10.1016/j.jsb.2006.03.009
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Comparative analysis of coiled-coil prediction methods

Abstract: In this study we compare commonly used coiled-coil prediction methods against a database derived from proteins of known structure. We Wnd that the two older programs COILS and PairCoil/MultiCoil are signiWcantly outperformed by two recent developments: Marcoil, a program built on hidden Markov models, and PCOILS, a new COILS version that uses proWles as inputs; and to a lesser extent by a PairCoil update, PairCoil2. Overall Marcoil provides a slightly better performance over the reference database than PCOILS … Show more

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Cited by 151 publications
(125 citation statements)
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“…Often the highest scores were at the N terminus as expected, but this domain was spuriously predicted elsewhere in the protein as well. For example, a typical false positive was found in the polyglutamate repeat in the LRR of Hero, which cannot physically form a coiledcoil (Ernst et al 2002;Gruber et al 2006). We do not attempt to distinguish between regular coiled-coils and the leucine zipper subclass, but note that many leucine zippers reported in the R-gene literature were not predicted to be coiled-coils, even though a requisite pattern of leucine residues was present.…”
Section: Resultsmentioning
confidence: 99%
“…Often the highest scores were at the N terminus as expected, but this domain was spuriously predicted elsewhere in the protein as well. For example, a typical false positive was found in the polyglutamate repeat in the LRR of Hero, which cannot physically form a coiledcoil (Ernst et al 2002;Gruber et al 2006). We do not attempt to distinguish between regular coiled-coils and the leucine zipper subclass, but note that many leucine zippers reported in the R-gene literature were not predicted to be coiled-coils, even though a requisite pattern of leucine residues was present.…”
Section: Resultsmentioning
confidence: 99%
“…2). The highest propensity to form a coiled coil was calculated (using the program PCOILS [5]) for the region from residue 24 to 69, followed by the region from residue 87 to 107 (Fig. 2).…”
Section: Methods (I) Cloning Expression and Purification Of Proteinsmentioning
confidence: 99%
“…HHalign reported a weak similarity (E50.015) between a short region of P4 within its coiledcoil domain (aa 316-348 in RBLV P4) and the last two helices of the DnaK peptide-binding domain. Thus, the suggested similarity between P4 and DnaK is probably not authentic, as it is not statistically significant and occurs within the coiled-coil region, which is known to provoke spurious hits in similarity searches with unrelated helical proteins (Ferron et al, 2006;Gruber et al, 2006).…”
Section: Comparison With Previous Studiesmentioning
confidence: 99%