
IPC 2.0 (isoelectric point calculator)
Calculate protein and peptide pI values using validated pKa scales and sequence models.
Input
What is IPC 2.0?
The isoelectric point (pI) is the pH where a protein or peptide carries zero net charge. It determines how a molecule behaves during isoelectric focusing, ion exchange chromatography, and 2D gel electrophoresis. Predicting pI from sequence requires knowing the pKa of every ionizable group, which varies depending on the pKa scale used.
IPC 2.0 (Isoelectric Point Calculator 2.0) by Kozlowski combines 19 pKa scales with machine learning to predict pI more accurately than any single Henderson-Hasselbalch calculation. The SVR models trained on 2,324 proteins and 119,092 peptides achieve RMSD values of 0.85 and 0.23 respectively. A SepConv2D deep learning model pushes peptide accuracy further (RMSD 0.22). Version 2.0 also introduced per-residue pKa prediction, estimating the dissociation constant of each ionizable residue in context using an MLP-SVR ensemble.
When to use IPC 2.0 vs simpler calculators
For a quick fixed-model estimate, the pI Calculator runs in the browser using fixed EMBOSS pKa values. Protein Parameters provides a broader sequence property report. IPC 2.0 is the better choice when:
- Accuracy matters (SVR and DL models outperform any single pKa scale)
- Comparing predictions across multiple scales helps assess confidence
- Per-residue pKa values are needed for understanding charge distribution
- Batch processing hundreds of sequences at once
How to use IPC 2.0 online
IPC 2.0 on ProteinIQ predicts the isoelectric point of proteins and peptides from amino acid sequence. Paste sequences in FASTA format (or fetch them from UniProt), choose a prediction method, and get pI values across up to 19 pKa scales plus machine learning predictions. The residue pKa predictor reports D, E, H, K, Y, and terminal sites; it does not predict cysteine or arginine side-chain pKa.
Pricing
A run costs 1 credit for the selected predictor. Predictor and scale selection do not change this price. The exact quote appears before submission.
Inputs
| Input | Description |
|---|---|
Protein/Peptide Sequences | One or more amino acid sequences in FASTA format. Also accepts .fasta, .faa, .fa, .fas, .txt, or native .csv datasets. UniProt IDs can be fetched directly using the batch fetcher. |
FASTA preserves full descriptions and ignores lines beginning with #. FASTA and CSV sequences require uppercase amino acid letters without stop symbols or gaps. Native FASTA and CSV readers substitute B with N, Z with Q, and U with C. Plain sequence text accepts lowercase letters through its native parser.
For pI CSV, use two columns: exp_pI,sequence. The first column contains an experimental pI value for each sequence. Residue pKa CSV uses the native 12-column dataset layout: pKa,uncertinity,pdb,chain,aa,position,monomer,trimer,pentamer,heptamer,nonamer,sequence. Select IPC2_pKa for this dataset. Deep learning CSV runs require at least 15 rows. A pI CSV run returns pI results; residue pKa requires its own dataset or sequence input.
The file limit is 50 MiB. Free accounts can submit up to 25 sequences and Lite accounts up to 1,000; the workspace applies the current plan limits before submission.
Settings
| Parameter | Type | Default | Description |
|---|---|---|---|
Predictor (method) | enum | IPC1_ALL | Select a native pI predictor, all pI predictors, residue pKa only, or the IPC1 report. |
IPC1 pKa scale (scale) | enum | ALL | Select any of the 19 listed scales or all scales. This controls the IPC1 report; trained models retain their fixed native feature sets. |
Predictor options
| Predictor | Best for | What it does |
|---|---|---|
IPC1_ALL | General use | Henderson-Hasselbalch with all 19 pKa scales (18 literature scales + ProMoST). Fastest option. |
IPC2_SVR_protein | Proteins | SVR trained on 2,324 proteins from SWISS-2DPAGE and PIP-DB. Reports all 19 scales plus the SVR prediction. |
IPC2_SVR_peptide | Peptides | SVR trained on 119,092 peptides from HiRIEF experiments. Reports all 19 scales plus the SVR prediction. |
IPC2_DL_peptide | Peptides | SepConv2D deep learning model. Sequences above 60 residues undergo native truncation; the report retains the sequence used for prediction. |
ALL | Method comparison | Runs IPC1, both SVR predictors, and peptide deep learning. Sequence inputs also receive residue pKa predictions. |
IPC2_pKa | Residue analysis | Runs the 9-MLP plus SVR residue pKa predictor without pI prediction. Supports the native residue pKa CSV dataset. |
IPC1_REPORT | Classical report | Runs the original IPC1 FASTA report with molecular weight and native average pI. Includes a 2D-PAGE PNG when the native density calculation can generate it. |
Results
The Results tab shows a spreadsheet with one row per sequence:
| Column | Description |
|---|---|
ID | Full sequence description from the FASTA header, or the native plain-input description. |
Length | Number of amino acid residues. |
MW | Molecular weight in Daltons. |
pI_[scale] | Predicted pI for each pKa scale (e.g., pI_IPC2_protein, pI_Bjellqvist, pI_ProMoST). |
pI_SVR_protein | SVR prediction optimized for proteins (when SVR or ALL method selected). |
pI_SVR_peptide | SVR prediction optimized for peptides (when SVR or ALL method selected). |
pI_DL_peptide | Deep learning prediction (when DL or ALL method selected). |
Avg_pI | Average pI across all calculated scales (excluding Patrickios). |
The Per-Residue pKa tab shows the sites reported by the native residue predictor. For FASTA with D, E, H, K, or Y at either end, native alanine padding changes the report sequence and position numbering. These positions are retained without conversion to original sequence positions:
| Column | Description |
|---|---|
Sequence | Which input sequence this residue belongs to. |
Position | Native 1-based position in the reported sequence, including terminal alanine padding. The native site and sequence are retained as additional columns. |
Residue | Amino acid type (D, E, H, K, Y, or the terminal residue). |
pKa | Predicted dissociation constant from the MLP-SVR ensemble. |
Downloadable outputs
Native predictor reports are available as FASTA, CSV, or residue pseudo-FASTA, alongside ipc2_results.json and run.log. The pseudo-FASTA report has three lines per record: description, native sequence, and semicolon-separated residuePosition_pKa sites. IPC1 reports retain three decimal places; SVR and residue pKa reports retain five. Deep learning follows the precision written by its native report.
The JSON file contains the spreadsheet projection. For comparisons requiring the complete native result, use the predictor report. The IPC1_REPORT plot is conditional on the native density calculation; small or degenerate datasets may produce no PNG.
Interpreting pI values
Most proteins have pI between 4 and 10. Knowing where a protein falls relative to pH 7 determines its behavior in common buffers:
| pI range | Character | At pH 7.4 (physiological) |
|---|---|---|
| <5 | Strongly acidic | Net negative charge |
| 5 to 7 | Weakly acidic | Slight negative charge |
| 7 to 9 | Weakly basic | Slight positive charge |
| >9 | Strongly basic | Net positive charge |
Differences between pKa scales show sensitivity to the chosen constants. Agreement is not a calibrated confidence score. The protein and peptide SVR models were trained on different experimental datasets, so choose the model appropriate to the sequence and validate consequential conclusions experimentally.
Deep learning can produce values outside the usual pI range for long or highly charged sequences. ProteinIQ preserves the reported values. For proteins, compare the protein SVR result rather than treating a truncated peptide-model prediction as a reliable pI estimate.
Interpreting per-residue pKa
Per-residue pKa values show how sequence context shifts each ionizable group's dissociation constant away from its "standard" textbook value. For example, an aspartate surrounded by other negative residues will have a higher pKa (harder to deprotonate), while one near positive charges will have a lower pKa.
These values are useful for identifying residues with unusual protonation behavior, which matters for enzyme active sites, pH-dependent conformational changes, and designing mutations that shift pI.
How does IPC 2.0 work?
Henderson-Hasselbalch method
The classical approach calculates net protein charge as a function of pH using:
Starting at pH 6.51, a bisection algorithm adjusts pH up or down until the sum of positive charges (Lys, Arg, His, N-terminus) equals negative charges (Asp, Glu, Cys, Tyr, C-terminus) within a precision of 0.01 pH units.
Each pKa scale assigns different dissociation constants to these groups, producing different pI estimates. The Bjellqvist scale additionally uses position-specific pKa values for N-terminal and C-terminal residues (e.g., N-terminal Ala has pKa 7.59 instead of the generic 7.5), which matters for proteins starting with A, M, S, P, T, V, or E.
ProMoST uses a separate model with three pKa values per residue (N-terminal, middle, C-terminal positions), giving it slightly different behavior from the other 18 scales.
pKa scales
IPC 2.0 includes 19 pKa scales:
| Scale | Origin |
|---|---|
IPC2_protein | Optimized for proteins (Kozlowski 2021) |
IPC2_peptide | Optimized for peptides (Kozlowski 2021) |
IPC_protein | Original IPC scale (Kozlowski 2016) |
IPC_peptide | Original IPC scale (Kozlowski 2016) |
ProMoST | Position-specific model (Halligan 2004) |
Bjellqvist | 2D electrophoresis standard with terminal corrections |
EMBOSS | EMBOSS software suite |
DTASelect | Proteomics analysis |
Grimsley | Experimental NMR measurements |
Lehninger | Biochemistry textbook |
Solomon | Protein chemistry |
Sillero | Theoretical calculations |
Rodwell | Biochemistry reference |
Thurlkill | NMR measurements in pentapeptides |
Toseland | Statistical analysis of PDB structures |
Nozaki | Model compound measurements |
Dawson | Data compilation |
Wikipedia | General reference values |
Patrickios | Simplified (only D/E/K/R, ignores C/H/Y) |
The Avg_pI column averages all scales except Patrickios, whose simplified model (ignoring cysteine, histidine, and tyrosine) makes it an outlier.
Support vector regression
The SVR models take a 19-dimensional feature vector (pI predictions from all 18 H-H scales + ProMoST) and feed it into a support vector machine with RBF kernel. The protein SVR was trained on 2,324 proteins from SWISS-2DPAGE and PIP-DB. The peptide SVR was trained on 119,092 peptides from high-resolution isoelectric focusing (HiRIEF) experiments.
Because the SVR sees all 19 scale predictions simultaneously, it learns which scales are most informative for different sequence compositions. It consistently outperforms any individual scale.
SepConv2D deep learning
The deep learning model uses a separable convolutional architecture with four input channels:
- One-hot encoding: 22 x 60 matrix of amino acid identity
- AAindex features: 15 physicochemical indices per position plus hydrophobicity
- Composition vector: Amino acid counts repeated across sequence length
- IPC predictions: pI from all scales + SVR, giving the model calibrated priors
Sequences longer than 60 residues undergo truncation that preferentially removes non-charged residues (Ala, Gly, Leu, etc.) while preserving ionizable residues that determine pI. This truncation uses random selection among non-charged positions, so predictions for long sequences may vary slightly between runs.
Per-residue pKa (MLP-SVR ensemble)
The per-residue pKa predictor estimates the dissociation constant of each ionizable residue (D, E, H, K, Y) plus the N- and C-terminal groups. It uses a stacking ensemble of 9 multilayer perceptrons (MLPs) feeding into a final SVR:
- 6 sequence-only MLPs operating on 5-mers through 15-mers around the target residue
- 3 AAindex-augmented MLPs operating on 3-mers through 7-mers
Each MLP encodes the local sequence context around an ionizable residue using one-hot encoding (and optionally AAindex physicochemical features). The 9 MLP predictions are stacked as features for the final SVR, which outputs a single pKa value. Charged N- and C-terminal residues are flanked with alanine padding before prediction to ensure they are treated as terminal groups.
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