Explain the Titration Curve of Lysine
Q: Draw the zwitterion for the amino acid backbone of: glycine alanine proline
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Q: Sketch out a structure of tyrosyl-glycyl-lysine at a pH of 13
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Q: Explain the Titrimetric profile of Lysine in figure 2
A: The isoelectric point is the pH at which any amino acid or protein has no net charge and thus will…
Q: Calculate the pI for the following tri-peptide: Glu-Arg-Lys
A: pI or isoelectric point is the pH at which a peptide or molecule is electrically neutral. The pH of…
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A: Nucleic acids are macromolecules. These are of two types - Deoxyribonucleic acid (DNA) and…
Q: The pH at which the Lysine R-group is 20 % dissociated is:
A: Option a) is correct Answer
Q: Draw all the possible tripeptides of serine, methionine, and glycine and name them.
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Q: draw a peptide bond of: glycine alanine proline
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A: (a) Tyrosine : It is an amino acid that is naturally produced in the body from another amino acid…
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A: Melting temperature of primer can be defined as a temperature at which one half of the DNA double…
Q: Explain the Titration profile of Lysine
A: Titration is a basic process which is used to analyse a sample. It is basically used to determine…
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Q: discuss the absorption spectra of the 3 amino acids Arginine, Leucine and Proline.
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Q: Describe lysine degradation.
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Q: Draw the dipeptide alanylvaline
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Q: raw the complete structure of the tetrapeptide Val-Cys-Glu-Ser.
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Q: Draw the α-l-glucopyranose sugars using Haworth projections:
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Q: Arginine exists in two high-pH forms instead of the usual one. Explain why.
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Q: Given the polypeptide chain below: Ala-Arg-Val-His-Asp-Gln 1. What kind of polypeptide is it? 2.…
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Q: Draw the titration curves for the following AA’s: Aspartic acid, Alanine, Lysine, Valine, Serine,…
A: Hi! Thank you for the question. As you have posted a question with multiple subparts, I will be…
Q: NH2 N- но-Р-О 'N' ОН ОН ОН
A: A is incorrect. Reason : Adenosine does not have any phosphate group in it's structure.
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Q: Drew the peptide sequence and write its full name Cys-Gln-Lys-His-Ala-Ser-Gln
A: All the amino acids mentioned in the question are linked Together by peptide bonds that is CONH. A…
Q: Draw the Titrimetric profile of Lysine
A: Lysine is one of 10 essential amino acids. It is a linear, positively-charged amino acid.
Q: Would the tetrapeptide W-X-Y-Z have the same pl as a peptide Z-Y-X-W? Why or why not?
A: The isoelectric point is the pH at which any molecule (here it would be the amino acids) carries no…
Q: с" CH2 CH2 "НaN H с. CH С" CH Нзс CHз ZI о-о
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Q: Draw the peptide formed between asparagine and histidine. H,N-CH-ċ-OH H,N- -CH—С—он CH2 ČH2 N° NH2…
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Q: Explain why Proline is seen as an exception when a ninhydrin complex is formed.
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Q: Spell out the name of the polypeptide using three letter codes for each amino acid separated with…
A: Phenyl isothiocynate is the Edman reagent. It reacts with N-terminal amino acid to give phenyl…
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- You want to treat 10 mL of HL-60 cells with cycloheximide in order to determine the half-life of a newly discovered protein. In order to do this, the final concentration of cycloheximide needs to be 90 µM. How much of a 150 mM stock solution of cycloheximide should you add to your cells?Please calculate and plot the charge on a peptide with the sequence of NEYK over the pH range from 1 to 13. Please use the pKa values from the table. You may calculate the charge at 1 pH unit intervals.Why different amino acids have different Rf values? If you separate a mixture of amino acids consist of glutamic acid, histidine, glycine, tryptophan and isoleucine with paper chromatography using NH3: Benzene (10:90) as a mobile phase what do you expect the Rf values of the amino acids will be?
- calculate the volume of stock solutions required to make up the buffer solutions that will be used for protein purification. The solutions you need to prepare for purification are: i. Binding Solution A: make up 50 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 5mM imidazole, 5% (v/v) glycerol ii. Wash Solution B: make up 50 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 75mM imidazole, 5% (v/v) glycerol iii. Elution Solution C: make up 10 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 500 mM imidazole, 5% (v/v) glycerol please show your working . Thnk youThe OXA-M290 protein is next purified by size exclusion chromatography. To determine the best type of size exclusion resin to use, the size of OXA-M290 must first be determined. Earlier, you determined the amino acid sequence of OXA-M290 (MRVLALSAVFLVASIIGMPAVAKEWQENKSWNAHFTEHKSQGVVVLWNENKQQGFTNNLKRANQAFLPASSAKIPNSLIALDLGVVKDEHQVFKWDGQTRDIATWNRDHNLITAMKYSVVPVYQEFARQIGEARMSKMLHAFDYGNEDISGNVDSFWLDGGIRISATEQISFLRKLYHNKLHVSERSQRIVKQAMLTEANGDYIIRAKTGYDTKIGWWVGWVELDDNVWFFAMNMDMPTSDGLGLRQAITKEVLKQEKIIP). Based on the amino acid sequence, what is the molecular weight of this protein? You can use the free ProtParam tool (https://web.expasy.org/protparam/) to calculate the molecular weights of proteins. Make sure to include units in your answer. Note: The amino acid sequence reported earlier does not include the His-tag that was added to OXA-M290 by the pET-28a vector. However, you do not need to consider the amino acids in the His-tag in your answer to this question. For Context ONLY: For…In a mixed heteropolymer experiment, messages were createdwith either 4/5C:1/5A or 4/5A:1/5C. These messages yielded proteinswith the amino acid compositions shown in the followingtable. Using these data, predict the most specific coding compositionfor each amino acid.4/5C:1/5A 4/5A:1/5CPro 63.0% Pro 3.5%His 13.0% His 3.0%Thr 16.0% Thr 16.6%Glu 3.0% Glu 13.0%Asp 3.0% Asp 13.0%Lys 0.5% Lys 50.0% 98.5% 99.1%
- You are trying to determine the PTMs on your protein of interest, so you set up a mass spectrometry experiment. You get the following data. Starting sequence: PRTEINSKICKASSDER After Trypsin digest, you get the following major peptides and weights from MS: TEINSKICK/1167 Da ASSDER/664 Da a. Which of these peptides is modified? b. What is the modification?Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.71; Pk2 = 10.78; PkR = 8.33 His: Pk1 = 1.82; Pk2 = 9.17; PkR = 6.0 Lys: Pk1 = 2.18; Pk2 = 8.95; PkR = 10.53 draw the protonic equilibria for the tripeptide what is the IpH? What is the dominant structure at pH 2.0? What is the first buffering region of the tripeptide?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
- Considering the chemical characteristics of the amino acids valine and glutamic acid (see Figure 5.14), propose a possible explanation for the dramatic effect on protein function that occurs when valine is substituted for glutamic acid.Please help! Sketch a titration curve of the peptide Ala-Tyr-Gln-Met-Asp-His from pH=0 to 14 up to 5 equivalnets of KOH (Please type answer)Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.71; Pk2 = 10.78; PkR = 8.33 His: Pk1 = 1.82; Pk2 = 9.17; PkR = 6.0 Lys: Pk1 = 2.18; Pk2 = 8.95; PkR = 10.53 What is the dominant structure at pH 2.0? What is the first buffering region of the tripeptide?