Chemistryhelp both and ill give thumbs up thank you Consider the peptides Pro-Gin-Val-Phe-His-Asp-Cys and His-Gln-Pro-Cys-Asp-Phe-Val. How do these two peptides differ?(Select all that apply.)The two peptides have different compositions.The two peptides have different isoelectric points.The two peptides have different titration curves.The two peptides differ in amino acid sequence.Submit AnswererencourTry Another Version 2 item attempts remaining If you were to have a mythical amino acid based on glutamic acid, but one in which the hydrogen that is attached to the y-carbon were replaced by another amino group, whatwould be the predominant form of this amino acid at pH 12 if the pKa value were 10 for the unique amino group?(Select all that apply.)OBoth of the carboxyl groups are deprotonated.The amino acid carries a negative 2 charge.The amino acid carries a negative 4 charge.The amino groups are in the form -NH.Both of the amino groups are deprotonated.Submit AnswerTry Another Version 2 item attempts remaining

Consider the peptides Pro-Gin-Val-Phe-His-Asp-Cys and His-Gln-Pro-Cys-Asp-Phe-Val. How do these two peptides differ? (Select all that apply.) The two peptides have different compositions. The two peptides have different isoelectric points. The two peptides have different titration curves. The two peptides differ in amino acid sequence. Submit Answer Try Another Version 2 item attempts remaining

Consider the peptides Pro-Gin-Val-Phe-His-Asp-Cys and His-Gln-Pro-Cys-Asp-Phe-Val. How do these two peptides differ? (Select all that apply.) The two peptides have different compositions. The two peptides have different isoelectric points. The two peptides have different titration curves. The two peptides differ in amino acid sequence. Submit Answer Try Another Version 2 item attempts remaining

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

If you were to have a mythical amino acidbased on glutamic acid, but one in which the hydrogen that isattached to the g-carbon were replaced by another amino group,what would be the predominant form of this amino acid at pH 4,7, and 10, if the pKa value were 10 for the unique amino group?
To calculate the isoelectric point of amino acids having other ionizable functional groups, we must also take into account the pk, of the additional functional group in the side chain. For an acidic amino acid (one with an additional acidic OH group): For a basic amino acid (one with an aditional basic NH group): pK, (a-COOH) + pK, (second COOH) - pKa (a-NH3") + pK, (side chain NH) pl = a. Indicate which pK, values must be used to calculate the pl of each of the following amino acids: [1] glutamic acid; [2] lysine; [3] arginine. b. In general, how does the pl of an acidic amino acid compare to that of a neutral amino acid? c. In general, how does the pl of a basic amino acid compare to the pl of a neutral amino acid?
A mixture of Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74), Phenylalanine (pl 5.48) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2. v First 1. Aspartic Acid v Second 2. Histidine v Third 3. Lysine 4. Phenylalanine v Fourth 5. Threonine v Fifth 6. No separation
Draw the Ala-Ser-Leu-Asp polypeptide (perspective formula) showing the fully extended backbone geometry (all angles +/- 180°). Include correct stereochemistry for L-amino acids. Label all bond rotations representing the angles at each residue
Draw a peptide that includes Phenylalanine, Cysteine, Tyrosine and Tryptophan. Label them by name and abbreviation. Assume a pH of 7 when drawing the protonation state of ionizable chemical groups. Why do the aforementioned aminoacids absorb U-V light?
1) All L amino acids have an S absolute configuration except L-cysteine, which has the R configuration. Explain what is unique about L-cysteine that would cause it to be designated as having an R absolute configuration despite sharing a similar three-dimensional structure with the other L amino acids.
Sketch a titration curve for the following amino acids and indicate the pKa values for all titratable groups. Also indicate the pH at which this amino acid has no net charge. aspartic acid gly-val
Given the following peptide, answer following questions 1-5: CO CH2 O || CH2 O H3N-CH-C-NH- CH-c-OCH3 | 1. Is this a dipeptide or tripeptide? 2. How many amino acid components/residues are there? 3. Name these amino acids. 4. What kind of bond links these amino acids? 5. The above structure represents the major ingredient in some commercial product(s). Identify the name of this major ingredient or the commercial product(s). Given that the hemagglutininin protein in influenza virus contains a remarkably long a-helix with 53 residues, answer questions 6-7. 6. How long is this a-helix (in nm)? Show all calculations. 7. How many turns does this helix have? Show all calculations.
Each ionizable group of an amino acid can exist in one of two states, charged or neutral. The electric charge on the functional group is determined by the relationship between its pKa and the pH of the solution. This relationship is described by the Henderson-Hasselbalch equation. a Histidine has three ionizable functional groups. Complete the equilibrium equations by assigning the proper pK₁ for each ionization and the net charge on the histidine molecule in each ionization state. H || H₂N-C-C-OH | CH₂ 2 + HN -1 -NH pKa = 1.8 +2 || H₂N-C-C-0- 1 CH₂ + HN -NH pKa = 9.17 Answer Bank pK₂ = 7.59 H|| H₂N-C-C-0- | CH₂ N pKa -NH = 6.0 -2 н II H₂N-C-C-0- | CH₂ +1 N C -NH 0
The peptide aspartyl-glutamyl-leucyl-threonyl-alanine, shown in the sketch drawing window, has several ionizable groups. Adjust the charges to show the molecule as it would exist at pH 5.00. Use the pk values in the table below. pK, Values for Ionizable Groups of Amino Acids. Amino Acid pA, of a-COOH pA, of e-NH, pA, of Side Chain Isoelectric Point (pI) Alanine 235 9.87 6.11 Arginine 2.01 9.04 12.48 10.76 Asparagine 2.02 8.80 5.41 Aspartic acid 210 9.82 3.86 298 Cysteine 2.05 10.25 8.00 5.02 Glutzmic acid 2.10 9.47 4.07 3.08 Glutamine 217 9.13 5.65 Glycine 235 9.78 6.06 Histidine 7.11 9.18 6.10 7.64 Isoleucine 232 9.76 6.04 Leucine 233 9.74 6.04 Lysine 218 8.95 10.53 9.74 Methionine 2 28 9.21 5.74 Phenylalanine 2 58 9.24 5.91 Proline 2.00 10.60 6.30 Serine 221 9.15 5.68 Threonine 2.09 9.10 5.60 Trуptophan 238 9.39 5.88 Tyrosine 2 20 9.11 10.07 5.63 Valine 2 29 9.72 6.00 • Use the wedge hash bond tools to indicate stereochemistry where it exists. • If a group is 2chiral, do not use…
A mixture of Asparagine (pl 5.41), Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2: v First 1. Asparagine v Second 2. Aspartic Acid 3. Histidine v Third 4. Lysine v Fourth 5. Threonine v Fifth 6. No separation
Place each charge form of alanine under the pH condition where it would be the predominant form. The pK₁ values for the carboxyl group and amino group of alanine are approximately 2.3 and 9.7, respectively. pH 11 H | H₂C-C-COO NH₂ Does not occur in significant amounts at any pH