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Handles chemical modification effectively by combining bio- and chemo-informatics handling of the molecules. pICalculaX can include modifications of peptides in isoelectric point (pI) calculations. It starts by analyzing the molecule and the pKa values of identified acidic or basic groups recorded and then predicts pI. The tool identifies the potential of hydrogen (pH) where the sum of partial charges is zero, by solving the Henderson-Hasselbalch equation for the ionization extent.
IPC / Isoelectric Point Calculator
A web service for the estimation of pI using different sets of dissociation constant (pKa) values, including two new, computationally optimized pKa sets. According to the presented benchmarks, IPC outperform previous algorithms by at least 14.9% for proteins and 0.9% for peptides (on average, 22.1% and 59.6%, respectively), which corresponds to an average error of the pI estimation equal to 0.87 and 0.25 pH units for proteins and peptides, respectively. Peptide and protein datasets used in the study and the precalculated pI for the PDB, SwissProt and some of the most frequently used proteomes are available for large-scale analysis and future development.
Allows the computation of various physical and chemical parameters for a given protein stored in Swiss-Prot or TrEMBL or for a user entered protein sequence. ProtParam permits users to select the portion of the sequence on which hewould like to perform the analysis when using a Swiss-Prot/TrEMBL entry. It integrates computing parameters such as the molecular weight, theoretical pI, amino acid composition, atomic composition, extinction coefficient, estimated half-life, and more.
pI calculator
Permits to calculate pKs values of phosphopeptides separated under different experimental conditions. pI calculator was created on the basis of an experimental dataset containing the most common Post-Translational Modifications (PTMs), such as oxidation, N-terminal acetylation, and phosphorylation. The tool allows user to choose the algorithm best suited for their experimental conditions. It is able to reveal correlation between the expected and experimental pI of modified peptides.
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