Analyze favorable residues, breakers, charge, and hydrophobic balance. View window scores and confidence notes immediately. Understand sequence regions likely to favor alpha helix formation.
Paste a raw sequence or FASTA text. Headers and unsupported characters are removed automatically.
This table uses the built-in sample sequence and default settings.
| Example Name | Sequence | Length | Average Propensity | Predicted Helix % | Longest Stretch | Best Window | Best Score | Verdict |
|---|---|---|---|---|---|---|---|---|
| Helix-rich peptide | MKALEEKLKALEEKLAALEGGQAL |
24 | 1.289 | 83.33% | 20 | LKALEE |
1.491 | Strong alpha helix tendency |
Average Pα = (Σ residue alpha propensity in window) / window size
Score = Average Pα - (breaker penalty × Gly/Pro count) - (I/V/T penalty × I/V/T count) + (salt bonus × salt bridge pairs) + (cap bonus × cap hits) + (hydrophobic moment weight × μH)
μH = sqrt((Σ hᵢ cos θᵢ)² + (Σ hᵢ sin θᵢ)²) / nHelix % = (predicted helix residues / total residues) × 100
This model is a rule-based estimator using residue propensities, breaker pressure, salt-pair balance, capping support, and amphipathic character. It is useful for screening and teaching, not for replacing experimental or deep-learning structure pipelines.
It estimates whether local sequence regions are favorable for alpha helix formation. The result is a propensity-based screen, not a solved three-dimensional structure.
No. This tool is much simpler. It focuses on alpha helix tendency using sequence rules, while full predictors model broader structural context and long-range interactions.
Both often weaken alpha helices. Proline disrupts backbone geometry, while glycine adds high flexibility that can reduce helical stability in many sequence contexts.
Helices form over local sequence segments rather than single residues alone. Sliding windows help detect continuous regions with enough collective support to sustain helical structure.
Hydrophobic moment measures amphipathic patterning across a helical face. It helps highlight windows whose residue arrangement supports a structured helical surface.
It can provide a rough hint, but membrane helices often need dedicated transmembrane models, stronger hydrophobic analysis, and topology-aware interpretation.
Breaker residues, strong beta-branched content, short runs, or a stricter threshold can lower the final score even when several residues have good intrinsic helix propensity.
The calculator accepts one-letter amino acid sequences and FASTA text. Unsupported letters, symbols, and numbers are removed before scoring.
Important Note: All the Calculators listed in this site are for educational purpose only and we do not guarentee the accuracy of results. Please do consult with other sources as well.