When the pH is below the pKa, that particular group will not have lost H+. Once the pH rises above pKa , H+ is lost.
For eg, pKa (NH3) = 9.13

So the structure of GlnCysAlaMet will be :

The NH3 + on the left side is still protonated since pH (7) < pKa (9.13).
The COOH on the extreme right has lost H+ to become COO- since pH (7) > pKa ( 2.13)
Draw the structure of the peptide GlnCysAlaMet at pH = 7.0 (Gln pka(NH3)= 9.13, Cys (SH)=8.3,...
6. A peptide has the sequence Cys-His-Phe-Glu-Ala-Arg a. Write the single letter sequence of the peptide b. Calculate the percentage and indicate the charge of the predominant peptide species at pH 6.5. Use the following pKa values: pKa Cys = 8.3, pKa N-terminus = 10.8, pKa His =6.0, pKa Glu = 4.3, pKa Arg = 12.5, pKa C-terminus =2.0 c. What is the charge of the peptide at pH 4.3? d. Draw the chemical structure of the predominant peptide species...
a) Draw the structure of a Gln-Lys-Met tripeptide at pH 7. b) Calculate the pl of the peptide. Show your work.
What is the approximate net charge of the following pentapeptide at pH 10? Arg-Gln-Cys-His-Ala What is the Isoelectric point (pI) of the peptide given above? Use the pKa values given here when needed: Side group/ amino acid pKa Asp 3.9 Glu 4.1 HIs 6.0 Cys 8.4 Tyr 10.5 Lys 10.5 Arg 12.5 C-term 3.5 N-term 9.0
An octapeptide contains the following amino acids: Met, Thr, Cys, Asp, Phe, Arg, Glu, Gln. Carboxypeptidase treatment of the octapeptide forms Asp and a heptapeptide. Treatment of the octapeptide with Chymotrypsin forms forms two tetrapeptides, A and B. Treatment of A with Trypsin yields two dipeptides, C and D. Edman degradation cleaves the following amino acids from each peptide: Cys (octapeptide), Cys (A), Gln (B), Cys (C), Glu(D). Partial hydrolysis of tetrapeptide B forms Gln-Thr in addition to other products....
An octapeptide contains the following amino acids: Met, Thr, Cys, Asp, Phe, Arg, Glu, Gln. Carboxypeptidase treatment of the octapeptide forms Asp and a heptapeptide. Treatment of the octapeptide with Chymotrypsin forms forms two tetrapeptides, A and B. Treatment of A with Trypsin yields two dipeptides, C and D. Edman degradation cleaves the following amino acids from each peptide: Cys (octapeptide), Cys (A), Gln (B), Cys (C), Glu(D). Partial hydrolysis of tetrapeptide B forms Gln-Thr in addition to other products....
Draw the structure of the dipeptide Lys-Glu at pH 7.0. Label the
following:
a) Peptide bond
b) N-terminus
c) C-terminus
d) An α-amino group and an ε-amino group
e) An α-carboxylate group and a Y-carboxylate group
Draw the structure of the dipeptide Lys-Glu at pH 7.0. Label the following: (a). peptide bond, (b). N-terminus, (c). C-terminus, (d). an a-amino group and an e-amino group, (e), an α-carboxylate group and a -carboxylate group.
Draw the following peptide at physiological pH. Gln-ser-his
Predict the charge on the major species of the peptide Ile–Arg–Asp–Ala–Lys–Ser–Gln at pH 7.0
The tetrapeptide Ac-Asn-Met-Cys-Lys has its N-terminus blocked by acetylation. Its C-terminal pKa is 4.30. The side chain pKa’s are 7.8 and 10.4. a. Write this peptide sequence using single letter abbreviations. b. Draw its predominant chemical structure at pH 8.0, including charges. c. What fraction of the peptide will exist in the predominant form at pH 8.0? (Discount any species that represent less than 1% of all species.) d. Calculate the pI of the peptide. e. If this tetrapeptide is...
Calculate the net charge of a peptide sequence W-S-N-G-C-H (all connected : Tryptophan-Serine-Asparagine-Glycine-Cysteine-Histidine) pKa values at (a) pH 2.0, (b) 6.0 (c) 7.0 and (d) 11.5. Assuming the ionisable groups have pKa values of His 6.0, Asp 3.6, Tyr 10.0, Cys 8.3, Arg 12.5, Lys, 10.5, Glu 4.3 C-term -COOH 2.0, N-term -NH3 + 9.5.