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STABLECOIL Ver.1
Created by B. Tripet and R.S. Hodges
STABLECOIL is a program designed to predict the location and stability of alpha-helical coiled-coil conformations within protein sequences. The program uses experimentally derived alpha-helical propensity and stability coefficients as reported by Zhou et.al., 1994, Wagschal et.al., 1999 and Tripet et.al., 2000. By summing the residue scores over a window width of 21, 28, 35 and 42, and comparing the total score to known globular and cytoskeletal coiled-coil containing sequences, the program displays the region and probability (in kcal/mol) that a particular sequence will adopt a coiled-coil conformation.
     
    Sequence Name
    sequence:
References:

Zhou, N.E., Monera,O.D., C.M. &R.S.Hodges (1994) alpha-helical propensities of amino acids in the hydrophobic face of an amphipathis alpha-helix. Protein and Pretide Letters, 1, 114-119.

Wagschal, K.,Tripet,B.,Lavigne,P., Mant, C. &R.S.Hodges, (1999). The role of position a in determining the stability and oligomerization state of alpha-helical coiled coils: 20 amino acid stability coefficients in the hydrophobic core of proteins. Protein Sci 8, 2312-2329

Tripet,B., Wagschal, K., Lavigne, P., Mant, C.T. and R.S. Hodges (2000). Effects of side-chain characteristics on stability and oligomerization state of a de novo designed model coiled-coil: Twenty amino acid substitutions in postions "d". J.Mol.Biol. (submitted).

STABLECOIL is described in:
Tripet,B. and R.S. Hodges (2000). STABLECOIL: Using stability data derived from model petides and de novo designed coiled-coils to predict the location and stability of native coiled-coils. J. Biol. Chem. (submitted).

Acknowledgements:

This program would not have been possible without finical support from PENCE and the excellent programming abilities of Leigh Willard, Robert Boyko and Lei Chen.