pepcoil
Function
Description
Coiled coils are formed by two or three alpha helices in parallel and in
register that cross at an angle of approximately 20 degrees, are
strongly amphipathic and display a pattern of hydrophilic and
hydrophobic residues that is repeated every seven residues. The seven
positions of the heptad repeat are designated a through g, a and d being
generally hydrophobic, while the others are hydrophilic.
The parallel two-stranded alpha-helical coiled coil is the most
frequently encountered subunit-oligomerization motif in proteins.
pepcoil calculates the probability of a coiled-coil structure for
windows of 28 residues through a protein sequence using the method of
Lupas A, van Dyke M & Stock J (1991); Science 252:1162-4
Usage
Command line arguments
Input file format
pepcoil reads in a protein sequence USA.
Output file format
Data files
None.
Notes
None.
References
-
Lupas A, van Dyke M & Stock J;
Predicting Coiled Coils from Protein Sequences.
Science 252:1162-4 (1991)
Warnings
None.
Diagnostic Error Messages
None.
Exit status
It always exits with a status of 0.
Known bugs
None.
Author(s)
Original program "PEPCOIL" by Peter Rice (EGCG 1991)
History
Target users
Comments