indicate which of the amino acid residues in the following peptide sequence contains a group that has a positive charge for its most likely charge state at pH 4. Lys-His-Thr-Glu-Asn-Cys-Val-Ile-Ser If none of the amino acids fit the criterion, select "none".) O Lys His

indicate which of the amino acid residues in the following peptide sequence contains a group that has a positive charge for its most likely charge state at pH 4. Lys-His-Thr-Glu-Asn-Cys-Val-Ile-Ser If none of the amino acids fit the criterion, select "none".) O Lys His

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Similar questions

Calculate the isoelectric point for below amino acid. asparagine: pKa (COOH) = 2.02; pKa (α-NH3+) = 8.80
Which peptides is more likely to take up on alpha-helical structure? Explain. Top: Leu-Lys-Ala-Glu-Asn-Asp-Glu-Ala-Ala-Arg-Ala-Met-Ser-Glu-Ala Bottom: Cys-Arg-Ala-Gly-Gly-Phe-Pro-Trp-Asp-Gln-Pro-Gly-Tyr-Ser-Asn
Considering the peptide structure on the image, label N-terminus and C-terminus, circle each of the peptide (amide) bonds, and provide the primary sequence of the protein using three letter abreviaciones for the amino acids
A peptide has the sequence Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly The p?a values for the peptide’s side chains, terminal amino groups, and carboxyl groups are provided in the table. Amino acid Amino pKa Carboxyl pKa Side‑chain pKa glutamate 9.609.60 2.342.34 4.254.25 histidine 9.179.17 1.821.82 6.006.00 tryptophan 9.399.39 2.382.38 serine 9.159.15 2.212.21 glycine 9.609.60 2.342.34 leucine 9.609.60 2.362.36 arginine 9.049.04 2.172.17 12.4812.48 proline 10.9610.96 1.991.99 Calculate the net charge of the molecule at pH 11 and estimate the isoelectric point (pI)(pI) for this peptide.
What are the structures of the amino acids that result from the hydrolysis of all the peptide bonds in the peptide? HO 'N' HO, NH2 H COOH draw structure ... draw structure ... draw structure .. left structure middle structure right structure
All amino acids have two ionizable functional groups: an α‑amino group (average pKa of 9.4) and an α‑carboxylic acid group (average pKa of 2.2). Aspartic acid has an ionizable side chain (R group) with a pKa of about 3.8. One of the possible ionization states of aspartic acid is shown in the image. At what pH would the structure be the predominant ionization state? Consider the ionization state of all three of the functional groups.
Proteins 1 and 2 interact strongly. A significant part of the interaction is between the amino acid side chains shown below. Protein 1= arginine C6H14N402 . Protein 2 = glutamic acid C5H9NO4 A mutation occurs in protein 2 that changes the amino acid shown above to one of the amino acids shown below. What change should disrupt the interaction between proteins 1 and 2 the most? the least? Protein 2- aspartic acid C4H7NO4, protein 2= Lysine C6H14N20 Protein 2= serine C3H7NO3 and protein 2= leucine C6H13NO2 aspartic acid would be the most and leucine would be the least aspartic acid would be the most and serine would be the least lysine would be the most and serine would be the least lysine would be the most and aspartic acid would be the least
the amino acid is tryptophan
His-Met-Asp-Tyr-Phe-Ser within this peptide, which amino acid residue is the most hydrophobic and why?