Peptide Fragment Ion Calculator

Enter a peptide sequence and choose fragment options. Compare charges, losses, and exact masses fast. Download neat tables for confident spectrum annotation and reporting.

Calculator

Format: C:57.02146,M:15.9949

Ion series
Neutral losses and fixed options

Example Data Table

Input peptide Mass type Ion Charge Example m/z Use case
PEPTIDE Monoisotopic b3 1+ 324.1554 N-terminal fragment check
PEPTIDE Monoisotopic y4 1+ 477.2191 C-terminal fragment check
ACDMK Monoisotopic b4-H2O 2+ 214.0820 Neutral loss review

Formula Used

Peptide neutral mass = sum of residue masses + H2O + terminal shifts + fixed residue shifts.

Fragment m/z = (neutral fragment mass + charge × proton mass) / charge.

b ions use the N-terminal residue sum. a ions are b minus CO. c ions are b plus NH3.

y ions use the C-terminal residue sum plus H2O. x ions add CO to the y style mass. z ions subtract NH3 from the y style mass.

Neutral loss rows subtract H2O or NH3 from the chosen base fragment before charge conversion.

How To Use This Calculator

  1. Enter the peptide sequence using standard one letter amino acid codes.
  2. Select monoisotopic or average masses.
  3. Choose ion series, charge range, neutral losses, and modification options.
  4. Add optional residue shifts using the residue:mass format.
  5. Press Calculate ions.
  6. Review the result table above the form.
  7. Download the CSV or PDF report when needed.

About This Calculator

Peptide fragment ions help explain tandem mass spectra. A peptide breaks at each backbone bond. The calculator lists common product ions for every valid split. It supports a, b, c, x, y, and z series. It also supports several charge states and neutral loss rows. This makes early spectrum checks easier.

Why Fragment Ions Matter

Proteomics software uses theoretical fragments to match measured peaks. A strong match can confirm peptide identity. It can also reveal missed cleavages, residue changes, or unexpected shifts. Manual review still matters. A clear ion table helps you inspect key peaks without opening a large search suite.

Advanced Inputs

Enter a clean amino acid sequence first. Remove spaces, numbers, and labels. Select monoisotopic masses for high resolution data. Use average masses for low resolution work. Add fixed carbamidomethyl cysteine when the sample was alkylated. Custom residue shifts can model oxidation, phosphorylation, or labeling. Terminal shifts let you test tagged peptides.

Reading The Results

Each row shows an ion label, charge, fragment sequence, neutral mass, and mass to charge value. The cleavage column shows where the peptide bond was cut. Loss rows show water or ammonia loss from the same base ion. Use the minimum and maximum mass filters to focus on the active scan range.

Good Practice

The output is theoretical. It does not predict intensity. Instrument type, collision energy, charge mobility, and residue chemistry all affect real spectra. Proline rich peptides often fragment in special ways. Acidic and basic residues can change peak balance. Use this table as a fast guide, then compare it with actual peak lists.

Export And Review

The CSV export is useful for spreadsheets and search notes. The PDF export is useful for lab records. Keep the entered options with each report. That makes later checks easier. When several settings are tested, save each table separately. Clear records reduce mistakes during annotation and reporting.

Limits To Remember

Some fragments may be unlikely. The tool still reports them for comparison. This is helpful during broad annotation. Use sensible charge settings for your instrument. Very high fragment charges may clutter the table. For routine work, start with one and two charges, then expand only when spectra show higher charged peaks.

FAQs

What is a peptide fragment ion?

It is a charged piece of a peptide formed during tandem mass spectrometry. Fragment ions help identify where a peptide backbone broke.

Which ion series are supported?

The calculator supports a, b, c, x, y, and z series. You can select one series or many series together.

Should I use monoisotopic or average masses?

Use monoisotopic masses for high resolution instruments and exact mass work. Use average masses for lower resolution review or older peak lists.

How are charge states handled?

The tool calculates each selected fragment from charge one through your maximum fragment charge. It then reports the matching m/z value.

What are neutral losses?

Neutral losses are small molecules removed from an ion. Common examples are water and ammonia. They can appear as extra peaks in spectra.

Can I add peptide modifications?

Yes. Add fixed residue shifts with residue:mass entries. You can also add terminal shifts and a carbamidomethyl cysteine option.

Why might results differ from my spectrum?

The calculator gives theoretical masses. Real spectra depend on ion intensity, collision energy, instrument settings, resolution, calibration, and peptide chemistry.

What does cleavage position mean?

It shows the peptide bond split used for that fragment row. For example, 3 / 4 means between residues three and four.

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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.