Amino Acid Charge at Neutral pH:
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The net charge of an amino acid is the sum of all positive and negative charges on the molecule at a given pH. At neutral pH (7.0), most amino acids have a net charge close to zero, except for those with ionizable side chains.
The calculator uses the Henderson-Hasselbalch equation to determine the charge state of each ionizable group:
Where:
Explanation: The calculator sums the charges from the amino group (positive), carboxyl group (negative), and any ionizable side chains.
Details: Knowing the net charge of amino acids is crucial for understanding protein behavior in electrophoresis, predicting protein solubility, and designing purification protocols.
Tips: Select the amino acid from the dropdown and enter the desired pH (typically 7.0 for physiological conditions). The calculator will show the predicted net charge.
Q1: Why do amino acids have different charges at different pH values?
A: The charge depends on protonation state of ionizable groups, which changes with pH according to their pKa values.
Q2: What is the isoelectric point (pI)?
A: The pH at which the amino acid has a net charge of zero. It's the average of the two pKa values that bracket the neutral form.
Q3: Which amino acids have charged side chains at neutral pH?
A: Aspartic acid, glutamic acid (negative), lysine, arginine (positive), and histidine (partially positive).
Q4: How accurate are these calculations?
A: They provide good estimates, but actual charges may vary slightly depending on local environment and temperature.
Q5: Can I use this for peptides?
A: This calculator is for single amino acids. Peptide charge calculation requires summing charges from all ionizable groups in the sequence.