Hd12108CO6st42000.5not text.only, no text.only, no text.11.5NaOH Equivalents22.5You create this titration curve of an amino acid.How many buffering zones are there? Enter a number, no letters.3A What is the pka1 of this amino acid? Enter only digitsWhat is the pka2 of this amino acid? DigitsAA/What is the pl of this amino acid? DigitsA/

Amino acids are biomolecules k that have an amino group, a carboxyl group and a side group linked to…

Answered: Hd 12 10 8 6 4 2 0 not text. 0.5 only,…

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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A protein that is normally found in an aqueous solution has these amino acids in its primary structure: glutamic acid, lysine, leucine, arginine, and tryptophan. Predict the location of each amino acid: in the interior portion of the protein (away from water) or on the outside of the protein (facing water). glutamic acid _________________________ lysine _________________________ leucine _________________________ arginine ________________________ tryptophan _________________________ Indicate whether each of the following statements describes a reversible competitive inhibitor, reversible noncompetitive inhibition, or an irreversible inhibitor. ________ a. It bonds covalently to the active site ________ b. The inhibitor effect can be reversed by the addition of more substrate ________ c. Inhibitor structure resembles that of the substrate ________ d. The inhibitor and substrate cannot bind to the enzyme simultaneously.
A protein that is normally found in an aqueous solution has these amino acids in its primary structure: glutamic acid, lysine, leucine, arginine, and tryptophan. Predict the location of each amino acid: in the interior portion of the protein (away from water) or on the outside of the protein (facing water). glutamic acid _________________________ lysine _________________________ leucine _________________________ arginine ________________________ tryptophan _________________________
A mixture of Alanine (pl 6.02), Glutamic Acid (pl 3.22), Glycine (pl 5.79), 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. Alanine v Second 2. Glutamic Acid v Third 3. Glycine v Fourth 4. Lysine v Fifth 5. Threonine 6. No separation
Examine the following peptide and the inserted table, and answer the 2 questions below: Thr-Glu-Pro-Ile-Val-Ala-Pro-Met-Glu-Tyr-Gly-Lys 1. Estimate the net charge of the peptide at pH 2.0. Explain. 2. Estimate the net charge of the peptide at pH 7.0. Explain.
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
A stock solution contains 0.2 mg/mL protein. From this stock solution, 179 uL is diluted with 1.1 mL buffer. What is the concentration of protein in this dilution?
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
a. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explain
Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEU I NEED IT ASAP PLEASE
In the figures are the titration curves of two amino acids. Consider the first titration. 00 000 pH 10.0 4 14.0 10 9 12.0 3 نیا 8.0 Select the pK, values of each functional group observed on the titration curve. 2 9 6.0 40 20 0.0 0.5 1.0 1.5 2.0 2.5 3.0 equivalents of [CH] Identify which amino acid is being titrated. arginine asparagine histidine lysine
Answer the questions regarding the tripeptide shown. H3N-CH- -C N-CH-C-N-CH-C-O | CH СНОН H CH2 H3C CH3 CH3 SH Which amino acid is the C-terminal amino acid? threonine cysteine methionine valine What is the name'of this tripeptide, using the three-letter amino acid abbreviations? Capitalize the first let
Identify the 20 amino acids and their corresponding three-letter and one-letter abbreviations

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