Q: (a) What is amino acid? Explain the function (or status) of an amino acid at pH 3 and 9. (b) What is…
A: a) Amino acid are organic compounds that contain amino ( -NH3+) and carboxylate ( - CO2-) along with…
Q: B. Show the structure of the following amino acids where the Zwitterion formed and calculate the pl.…
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Q: the percentage of dimethylphthalate (DMP) in the sample.
A: According to the question a sample containing a mixture of dimethylphthalate (DMP) , C6H4(COOH3)2…
Q: 9. How do you know if a malenimide based reagent will conjugate to nitrogen or sulphur in an amino…
A: we can identify the malenimide based reagent as amino acids by looking at the following - amino…
Q: 15. The quantitative determination of glutamic acid can be carried out: A) Kjeldahl method B)…
A: The structure of glutamic acid is
Q: 2. The a chain of haptoglobin exhibits genetic polymorphism since glu- tamic acid can be replaced by…
A: 2)First, we will see the difference between the SDS and Native polyacrylamide gel electrophoresis…
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Q: How To Use (R)-α-Methylbenzylamine to Resolve a Racemic Mixture of Amino Acids ?
A: The provided racemic mixture contains amino acid enantiomers. The (S)-form and (R)-forms react with…
Q: What alkene is needed to synthesize each amino acid by an enantioselective hydrogenation reaction…
A: The amino acid, alanine is formed by enantioselective hydrogenation of achiral alkene with hydrogen…
Q: A tripeptide on hydrolysis produced glycine, alanine and leucine. The structures of these amino…
A: Amino acids are the molecules that contains amino and carboxylic group along with a side chain…
Q: The initial pH of a 2M arginine solution is 14. What is the predominant structure of arginine in…
A: At pH = 14 , arginine exists in completely deprotonated form .
Q: Calculate the fraction of Asp that has its side chain protonated at pH 7.4
A: amino acid shows variation in protonated forms at different pH.
Q: Another strategy used to resolve amino acids involves converting the carboxy group to an ester and…
A: Two enantiomers of alanine amino acid are present i.e. S & R form of it.
Q: Explain why the pKa of the - NH3+ group of an a-amino acid is lower than the pKa of the ammonium ion…
A: In primary (1o) amine, RNH3+, the -NH3+ group is attached to the electron-donating group that is…
Q: Tyrosine gave a positive reaction to these tests except l. Hopkins-Cole |I. Biuret I.Sakaguchi IV.…
A: Hopkins Cole test - to detect tryptophan Biuret test - for present of peptide bond and…
Q: In the experiments of Barrick et al. (as shown), it was observed thatreplacement of histidine by a…
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Q: Using reaction equations, discuss the solubility of prilocaine in: a) Acidic aqueous environment b)…
A: Prilocaine(C13H20N2O) is a slightly polar basic amide with pKa = 7.89 or pKb = 6.11
Q: Doaw fae and mer igemer [RI(2-(m-todyalaze) pyidine),7
A:
Q: (b) Describe how the charge of some amino groups in a protein might differ at pH 9.0 and pH 5.0.…
A: Polypeptides are polymers of amino acids that make up proteins. The amino (–NH2) and carboxylic acid…
Q: me amino group = 9.04, and pKaR for the side chain - 12.48
A: Deprotection of groups depends upon the it's pKa value when pH > it's pKa then deprotection…
Q: Another strategy used to resolve amino acids involves converting the carboxy group to an ester and…
A: In alanine one stereogenic center is present. The carboxylic group of both enantiomers of alanine…
Q: Draw a formula for Thr-Ala-Ala (T-A-A) in its predominant ionic form at pH 7.3. You may assume for…
A: Here we are required to draw the structure of peptide predominant at pH 7.3
Q: Why is the pK of the carboxyl group of glycine (pK = 2.3) less than that for acetic acid (pK =…
A: because conjugation stabilization of the conjugate ACID. That extra proton is stable in the acidic…
Q: What is the K, of the amino acid leucine if it is 34.5% disso- ciated at pH = 9.46? |3D
A: “Since you have asked multiple question, we will solve the first question for you. If you want any…
Q: 10. Draw the full chemical structure of the tetrapeptide G-H-F-A as it would look at pH 12.0. Use…
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Q: This is a homework question... In nature, amino acids in proteins are typically found in the…
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Q: c) An essential amino acid with the systematic name 2-amino-3-phenylpropanoic acid. It has pka1 =…
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Q: 1A) Draw a peptide solely derived from L- amino acids. 1B) Note all stereocenters and assign R,S…
A: Isomers are the species that have the same molecular formula but due to differences in the molecular…
Q: Arginine has ionizable groups with pKa values of 2.17, 9.04, and 12.48. A researcher makes up 73 mL…
A: From the pKa values of arginine, it can be stated that, at pH 8.5 second proton is partially…
Q: Draw the zwitterion formula for the amino acid Ile. • You do not have to consider stereochemistry.…
A: The given amino acid is Isoleucin (Ile). The structure of Isoleucin is,
Q: A compound is known to have a free amino group with a pKa of 8.6, and one other ionizible group with…
A: The reaction representing 2 ionization of the compound with 2 pKa value
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Q: 81. Indicate beloging to glycofrangulin. I. aglycone part is frangulin II. it is aglycone III.…
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Q: 5. The purpose of SDS in SDS-PAGE is (a) to selectively bind the target protein. (b) to maintain…
A: SDS (sodium dodecyl sulphate) is an anionic detergent. SDS facilitates protein bifurcation. It…
Q: 13. You were provided with a trypsin stock solution of known enzymatic concentration of 0.75 ug/ml.…
A: Trypsin is a protease enzyme. It helps in biochemical reactions in the body. Its medication is…
Q: Another method to form a peptide bond involves a two-step process Reaction of the p-nitrophenyl…
A: Steps of synthesis is shown below:
Q: Draw a structural formula for the form of amino acid most prevalent at pH 1.0. (a) Arginine
A: Amino acids contain an amino group and a carboxyl group at the same carbon with a side chain (-R)…
Q: Another method to form a peptide bond involves a two-step process:[1] Conversion of a Boc-protected…
A: a) Nitro group is an electron withdrawing group. Here nitro group is present on para position of the…
Q: 31. The pK1, pK2, and pKr for the amino acid glutamate are 2.1, 9.5, and 4.1, respectively. At pH…
A: Answer - The correct option is (e)
Q: A solution of amino acid having carboxylic side chain was titrated against NaOH. If initial pH of…
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Q: Draw the product that valine forms when it reacts with di-tert-butyl dicarbonate and triethylamine…
A: Here
Q: Alanine is a diprotic amino acid with a pk, = 2.344 for the carboxylic group and a pka = 9.868 for…
A: Ajj
Q: The shaded area in the following diagram shows CH₂ CH₂ ? H N-HO -CH₂ C-OH-N Gly 193 H RN O Covalent…
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Q: . The _____________ plot shows the free energy change for a given amino acid window, allowing the…
A: Here we need a curve which shows the free energy change for a given amino acid window, allowing the…
Q: 7. Determine the net charge at pH 6 on each peptide shown below. The pKa's of relevant side chain…
A: We have to determine the net charge on the peptide
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Q: i) Draw the D- and L- isomer for tyrosine using Fischer projection ii) Sketch the titration curve…
A: Since you have asked multiple questions, we will solve the first question for you. If you want any…
Q: 13.) A mixture containing 50% mole of A is distilled at a temperature T, what is the distillate to…
A: In relation to molar concentration, mole fraction is temperature independent Here variation of…
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- Angiotensin II is a polypeptide that regulates blood pressure. 2nd attempt Enter the amino acids, in order, as three-letter abbreviations, separated by hyphens. Start at the N-terminal end. Which amino acids are in the structure? HN HN. NH₂ NH₂ НО. NH NH NH asp-arg-val-tyr-lle-his-pro-phet HO- NH HO- **** HN Angiotensin II NH NH See Periodic Table SeYou may use the following table of pKa values for typical amino acid substituents. alpha carboxylate group Sidechain carboxylate Imidazole alpha amino group Guanidino group First [Select] 2 [Select] 4 Thiol sidechain amino group Consider the following 3 peptides. Last 6 9 12 8 Peptide 1: E-H-A-D-E-K Peptide 2: E-D-R-H-Y-G Peptide 3: G-E-G-D-S-D What would be the order of elution of these peptides for a anion exchange column at pH 7.0? 11 [Select]Draw the structure of the protected amino acid that must be anchored to the solid support in order to use a Merrifield synthesis to prepare leucine enkephalin. Include stereochemistry in your answer. Do NOT explicitly draw any hydrogen atoms in your structure or use abbreviations like OMe, COOH or Ph. (N terminus) Try-Gly-Gly-Phe-Leu (C terminus) НО. H₂N ✔ Edit Drawing H₂C CH₂ OH
- Explain the order of elution (with a buffer of pH 4) of the following pairs of amino acids through a column packed with Dowex 50 a. aspartate before serine c. valine before leucine b. serine before alanine d. tyrosine before phenylalanineWhich of the following reagents is used to protect the amino group of the N-terminal residue in solution-phase peptide synthesis? 單選: O a. trifluoroacetic acid O b. benzyl chloroformate O c. dicyclohexylcarbodiimide O d. phenyl isothiocyanate O e. lithium diisopropyl amideA. Write the structure of the pentapeptide GLDSC. B. What is the complete name of this pentapeptide? Show a tertiary structure of ACGGC after a disulfide bond forms. A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin; the other was treated with cyanogen bromide. Given the following sequences (N-terminal to C- terminal) of the resulting fragments, deduce the sequence of the original peptide. Trypsin treatment Asn-Thr-Trp-Met-lle-Lys Gly-Tyr-Met-Gin-Phe Val-Leu-Gly-Met-Ser-Arg Cyanogen bromide treatment Gin-Phe Val-Leu-Gly-Met lle-Lys-Gly-Tyr-Met Ser-Arg-Asn-Thr-Trp-Met
- 5. A peptide is synthesized using a solid-phase peptide synthesis strategy. Amino acids are typically protected using a Boc group, Fmoc group or Cbz group. Which amino acids will require two protecting groups instead of one? A. E В. G С. L D. W E. F nswer: Explanation: 34%Explain the order of elution (with a buffer of pH 4) of the following pairs of amino acids through a column packed with Dowex 50a. aspartate before serine c. valine before leucineb. serine before alanine d. tyrosine before phenylalanineReaction of a polypeptide with carboxypeptidase A releases Met. The polypeptide undergoes partial hydrolysis to give the following peptides. What is the sequence of the polypeptide? 1. Ser, Lys, Trp 4. Leu, Glu, Ser 7. Glu, His 10. Glu, His, Val 2. Gly, His, Ala 5. Met, Ala, Gly 8. Leu, Lys, Trp 11. Trp, Leu, Glu 3. Glu, Val, Ser 6. Ser, Lys, Val 9. Lys, Ser 12. Ala, Met
- Which of the following reaction sequences could produce the (L)-amino acid Q in greater than 50% yield? I. Piom Ph OH Br I. only O I. and II. O I. and III. O I., II., and III. 1) xs NH3 2) H3O+ II. Ph Ph HN O NH3 Q O OH O OH 1) H₂, Pt 2) NaOH 3) H3O+ III. EtO O HN. O O OEt 1)NaOEt 2) PhCH₂Br 3) H₂O*, Ab. Draw phi-psi angles about a valine from a short peptide indicating: 1) a phi-angle of+100° and 2) a psi-angle of -45° . Use Newman projections and label your work clearly. (Note: the identity of the neighboring amino acids does not matter!)60 61 62 63 The peptide KNYPEH N-terminal amino group has a pKa of 8.6 and the C-terminal carboxylate group has a pKa of 4.5. What is the net charge of this peptide at a pH of 1? Type your answer... The peptide KNYPEH N-terminal amino group has a pKa of 8.6 and the C-terminal carboxylate group has a pKa of 4.5. What is the net charge of this peptide at a pH of 7? Type your answer... The peptide KNYPEH N-terminal amino group has a pKa of 8.6 and the C-terminal carboxylate group has a pKa of 4.5. What is the net charge of this peptide at a pH of 15? Type your answer... The peptide KNYPEH N-terminal amino group has a pKa of 8.6 and the C-terminal carboxylate group has a pKa of 4.5. What is the isoelectric point of this peptide? Type your answer... DU