Q.41 The net charge on the following peptide at pH 7.0 is _____ . Val-Asp-Asn-Lys-Ser-Ile

Q.41 The net charge on the following peptide at pH 7.0 is _____ .
Val-Asp-Asn-Lys-Ser-Ile

The net charge on the peptide Val-Asp-Asn-Lys-Ser-Ile at pH 7.0 is +1.

The net charge on peptide at pH 7 determines protein behavior in biochemical assays, crucial for CSIR NET Life Sciences preparation. This guide breaks down the calculation for Val-Asp-Asn-Lys-Ser-Ile using standard pKa values and Henderson-Hasselbalch principles.

Ionizable Groups

Peptides have charges from N-terminal amino (~pKa 9.0, protonated +1 at pH 7), C-terminal carboxyl (~pKa 2.0, deprotonated -1 at pH 7), and side chains where pH > pKa means deprotonated (acidic: -1; basic: 0) or pH < pKa means protonated (basic: +1).

  • Val (V): No charged side chain.

  • Asp (D): Carboxyl side chain pKa ~3.9, deprotonated -1 at pH 7.

  • Asn (N): Neutral amide side chain, charge 0.

  • Lys (K): Amino side chain pKa ~10.5, protonated +1 at pH 7.

  • Ser (S): Hydroxyl side chain pKa >13, neutral 0.

  • Ile (I): Hydrocarbon side chain, neutral 0.

Charge Calculation

Sum the charges: N-terminal (+1) + C-terminal (-1) + Asp side chain (-1) + Lys side chain (+1) = +1.

Group pKa State at pH 7 Charge
N-terminal NH3+ ~9.0 Protonated +1 
C-terminal COOH ~2.0 Deprotonated -1 
Asp side chain 3.9 Deprotonated -1 
Lys side chain 10.5 Protonated +1 
Others (Val, Asn, Ser, Ile) N/A Neutral
Net +1

CSIR NET Exam Tips

No options provided, but common distractors include forgetting terminals (-1 total), miscounting Asp/Lys (0 or +2), or assuming neutral side chains charged. Practice with pI tables: acidic residues lower pI, basic raise it. Verify using peptide calculators for confirmation.

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