Application: folding studies of the pheromone Er-10 from
Euplotes raikovi (38 amino acid residues).
- Ten tertiary structures of Er-10 were solved by NMR spectroscopy.
- Three-helix bundle (residues 2-8, 12-18 and 24-32) stabilized by
three disulfide bridges.
- Energy minimization calculations were performed with and without
protein-solvent interactions. Apolar solvation parameters were used
(
 i = 1 kcal/mol/Å2
for C and S; = 0 kcal/mol/Å2 for other atoms).
- Helical residues constrained to -72° <
 < -42° and
-62° <  < -32°.
S-S bridges not included.
- All 10 unrefined NMR structures and 25 random structures used
as starting geometries.
- RMSD values calculated for backbone atoms. Unrefined NMR structure
1 used as reference.
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