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PEPCOIL application details page
Predicts coiled coil regions
Coiled coils are formed by two or three alpha helices in parallel and inregister that cross at an angle of approximately 20 degrees, arestrongly amphipathic and display a pattern of hydrophilic andhydrophobic residues that is repeated every seven residues. The sevenpositions of the heptad repeat are designated a through g, a and d beinggenerally hydrophobic, while the others are hydrophilic. The parallel two-stranded alpha-helical coiled coil is the mostfrequently encountered subunit-oligomerization motif in proteins. pepcoil calculates the probability of a coiled-coil structure forwindows of 28 residues through a protein sequence using the method ofLupas A, van Dyke M & Stock J (1991); Science 252:1162-4
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