please help me understand asapPlease draw by hand a tripeptide of Glu, Gln, and 1 aminoacid of your choice (Not Glu or Gln again) at pH 7.0 and9.0. The only requirement is that the amino acid shouldbe 1 of the amino acids with ionizable R groups. Peptideshould have appropriate charges on groups. Please

A tripeptide is a peptide that was derived from amino acids joined by a peptide bond. where a…

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Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter26: Synthesis And Degradation Of Nucleotides

Section: Chapter Questions

Problem 22P

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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
Amino acid analysis of a decapeptide gave the following residues: Ala (2), Gly, Leu, Lys (2), Met, Phe, Trp, Val Subjecting the decapeptide to various chemical/ enzymatic hydrolysis yields the following fragments: Cyanogen bromide: Leu-Ala-Met and a heptapeptide Trypsin: Phe-Ala-Lys and a heptapeptide Chymotrypsin: Gly-Val-Lys-Phe, Ala-Lys, Leu, and a tripeptide • Thermolysin: Phe-Ala-Lys, Leu-Ala-Met, and two dipeptides . Note that the intact decapeptide was used in each treatment. 1. What is the sequence of the heptapeptide produced upon treatment with trypsin? Fill each blank with the three-letter designation of the amino acid residue from the N-terminus to the C-terminus. 2. What is the sequence of the tripeptide produced upon treatment with chymotrypsin? Fill each blank with the three-letter designation of the amino acid residues from the N-terminus to the C-terminus.
Amino acid structure For any ionizable group, indicate the pka value and draw the structure that would be expected at the pH inside the cell (~7.4).
Description Please draw the structure of the 19 L-a-amino acids and proline in any form, as you prefer. You may want to use a letter-size sheet or larger, it's up to you. Guiding principle: You want to understand the differences among amino acids. Although you may want to only draw the R-group it's preferable to draw it along with the rest of the molecule (i.e., the Ca, the amino group and the carboxyl group). Here are some examples (your drawings should not limited to the following styles): H₂C NH₂ OH shutterstock.com-222977980 Alanine H H Proline OH %%% lysine a alamy stock photo Tryptophan HN NH₂ shutterstock.com-1819000134 QH COOH H₂N-C- H CH ₂ Phenylalanine H₂N NH dreamstime.com arginine NH₂ OH
Determine the net charge (to the nearest integer) on the following peptide at pH 5 AND pH 12. Estimate the isoelectric point (pl) for this peptide: H2N-Leu-Gly-Lys-Glu-COOH Assume the pK,s for functional groups are: alpha-amino 6. alpha-carboxy sidechain-amino (Lys) 10.5 sidechain-carboxy (Glu) 4.2 O Net charge at pH 5 and 12 is 0 and -2, respectively, pl =6.6 O Net charge at pH 5 and 12 is 0 and -2, respectively, pl =3.1 O Net charge at plH 5 and 12 is +2 and -1, respectively, pl =7.5 O Nct charge at pH 5 and 12 is +1 and -1. respectively,. pl -4.5 2.
peptide Lys-Glu-Trp answer the following questions: Draw the structure of this peptide when all the ionizable groups are fully protonated. How many ionizable groups does this peptide have? Label the pKa for each of the ionizable groups in the structure above. Draw the appropriate titration curve for this peptide on graph paper starting at pH 0 and ending at pH 14. Label the x-axis, y-axis and the pKa Determine the overall net charge of this peptide at each full equivalent point (including 0) where the ionizable group is 100% deprotonated. Determine the pI for this peptide. Determine the average overall net charge of a mixture of this peptide in a solution where pH=8.5.
Quantitative Estimation of Amino Acids by Ninhydrin http://vlab.amrita.edu/?sub=3&brch=63&sim=156&cnt=2 can u help me with question 2 of the assignment questions Based on the experimental data provided, estimate the amount of amino acid in the given unknown solution by Ninhydrin method. SI No. Volume of standard amino acid solution (ml) Amount of amino acid (µg) OD at 570nm 1 Blank 0 2 0.2 0.12 3 0.4 0.25 4 0.6 0.45 5 0.8 0.55 6 1.0 100 0.68 7 Unknown (0.5ml) 0.41
Asp-Gly-Lys-Glu-Ile-Phe Draw its full chemical structure as it would exist at pH = 7.0. Draw an arrow pointing to each peptide bond. Identify the net charge of the peptide and briefly explain how you arrived at this answer.
1. Cysteine is an important amino acid that stabilizes the structure of peptides and proteins by the formation of disulfide bond with another cysteine residue. Illustrate the titrimetric profile of cysteine and calculate its isoelectric pH. [Hint: The sulfhydryl group is titratable] 2. The tripeptide Glu-Pro-Arg (EPR) which is a product of Lactobacillus casei fermentation of milk was found to have potent blood pressure lowering properties. Draw the structure of the tripeptide, give its systematic name, show its titration profile, and determine its isoelectric pH.
The amino acid that is often used as a tag (in a run of 6-8 of this amino acid in a row) for protein purification, at pH 5.0. Discuss the significance of the Ramachandran plot. Contrast the conformational states of Gly and Pro in proteins to those of other amino acid residues.
1.Ala-Phe-Lys-Val-Val-Glu From the above polypeptide, what amino acid/s go/goes inside the cell after the following treatment: Chemotrypsin, thermolysin, then finally pepsin. What protein is left undigested? Write the primary structure of the undigested protein? 2.K-V-F-W-P-L-A-Y a.Chemotrypsin treatment b.Trypsin treatment c.Pepsin treatment d.Thermolysin treatment 3.Total acid hydrolysis of a pentapeptide complemented by total alkalinehydrolysis yields an equimolar mixture of 5 amino acids listed alphabetically, ala-cys,lys,phe,ser. N-terminal analysis with phenylisothiocyanate (PITC) generate PTH-ser. Trypsin digestion produces a tripeptide where N-terminal residue is cys and a dipeptide with ser as its N- terminal.Chemotrypsin digestion of the above tripeptide yields ala plus another dipeptide. A.What is the amino acid sequence of the tripeptide B.What is the amino acid sequence of the dipeptide derived from trypsin digestion? C.What is the primary structure of the original…
5 For the peptide structure in #3, (ASP-ALA-THR-LYS-GLY), use the chart at the end of this HW set to: A. Determine the net charge of the pentapeptide at pH 3, 4, 7, 10 and 11. B. Estimate the isoelectric point, pl, for this 5-amino acid peptide

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