Draw a schematic of the chemical structure of the Leu-Tyr-Met-Lys tetrapeptide, with thecorrect ionization at neutral pH (pH 7). Also, give an estimate the pl of this tetrapeptide (youare given that the pKa of any acidic R group is 4, the pKa of any basic R group is 11.5, and thepKa of the α-COOH is 2, and the a-NH3 is 9.5). Provide rationale!

Structure of Leu-Tyr-Met-Lys at neutral pH (7) : At neutral pH (around 7), the ionization state of…

Answered: Draw a schematic of the chemical…

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

Calculate and draw the isoelectric point of the tetrapeptide Ser-Leu-Phe-Pro at pH 7.0. hand written please
For the following amino acids select the INCORRECT alternative: (a) At pH = 4 all migrate towards the cathode except Asp. (b) At pH = 10 all migrate towards the anode. (c) The pI of phenylalanine (Phe) will be about 5.5. (d) The pl of aspartic acid (Asp) will be about 2.8. (e) At pH = 7 the amino acids Arg and Lys migrate towards the cathode and the rest to the anode.
Consider a protein in which a negatively charged glutamic acid side chain (pKa=4.2) makes a salt bridge (ion-ion interaction) with a positively charged histidine side chain (pKa=6.5). Part C: Justify your answer with calculations of partial charges on these amino acid side chains at pH=7.9.(Hint: Consider lessons from Coulomb's law, and the Henderson-Hasselbalch equation.)
Phosphate buffers are commonly used to mimic biological systems. Given that phosophoric acid is a triprotic acid with three pKas (2.12, 7.21, and 12.32), why do you think this is? What are the dominant buffering compounds present in a phosphate buffer near physiological pH?
Trehalose, also known as mycose, is a disaccharide found in certain mushrooms. It is composed of two a-D-glucose linked in a aa(1à1) glycosidic bond. Using Haworth projection, draw the structure of trehalose. Indicate whether it is reducing or non-reducing.
The amino acid glycine is often used as an ingredient in buffers for biochemistry experiments. The amino group of glycine has a pKa of 9.6. Glycine exists in either a protonated form (-NH3+) or a free base (-NH₂). a) In what pH range can glycine be used as an effective buffer? b) In a 0.1M solution of glycine at pH 9.0, what fraction has its amino group in the protonated form? c) When 99% of the glycine is in the protonated from, what is the numerical relation between the pH of the solution and the pKa of the amino group?
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
Draw the two possible Haworth structures (both alpha and beta anomers) for the following monosaccharides and give their corresponding systematic names. [Show the stepwise process] (a) D- Fructose
Glucose-1-phosphate has a ΔG°′ value of −20.9 kJ/mol, whereas that for glucose-6-phosphate is −12.5 kJ/mol. After reviewing the molecular structures of these compounds, explain why there is such a difference in these values.
For the following pentapeptides: Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser A. Compute their isoelectric pH (pI). Show full solution. Use standard pKa values. B. Do these peptides with the same amino acid composition have different net charges at pH 7.0? Explain briefly. C. Would you expect the titration curves of the two peptides to differ? Why or Why not?
Given below is the name of a polypeptide Valyllysylalanylhistidylaspartylphenylalanylglycylglutamate The average pKas of different groups/side chains are shown in the table below: Group/amino acid side chain pKa C-terminus 3.5 3.9 E 4.1 H 6.0 8.4 Y 10.5 K 10.5 R 12.5 N-terminus 9.0 What is the total charge of this molecule at pH 5? [ Select ] What is the total charge of this molecule at pH 9.5? [ Select] > >
The amino acid arginine ionizes according to the following scheme: (a) Calculate the isoelectric point of arginine. You can neglect contributions from form I. Why? (b) Calculate the average charge on arginine when pH = 9.20. (c) Is the value of average charge you calculated in part b reasonable, given the pI you calculated in part a? Explain your answer

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