Guanidine and the guanidino group present in arginine are two of the strongest organic bases known. Account for their basicity.

Q: ОН S. NH2 HO NH2 Thyrosine (tyr) Methionine (met)

A: Zwitter ion- it is as ion possessing both positive and negative electrical charges.

Q: The cleavage pattern for o-lodosobenzoate is C-terminal to tryptophan; the cleavage pattern for…

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Q: lonization State of Histidine Each ionizable group of an amino acid can exist in one of two states,…

A: “Since there are multiple questions and it is not mentioned that which one has to be solved so I am…

Q: For each amino acid listed, tell whether its influence on tertiary structure is largely through…

A: Since we only answer up to 3 sub-parts, we’ll answer the first 3 sub-parts for you. Please resubmit…

Q: Show the mechanism and explain how the Ala-Val-Ile peptide bond is formed.

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Q: Draw the resonance forms of a protonated guanidino group, and explain why argininehas such a…

A: The structure of guanidine group is as follows,

Q: Explain the distinction between a general acid catalyst and a specific acid catalyst. Explain how an…

A: General  acid catalyst- General the acid catalyst is involved in an equilibrium prior to the…

Q: Explain the difference in the pKa values of the carboxyl groups of alanine, serine, and cysteine.

A: The compounds in which both amino (NH2) and carboxylic acid (COOH) group are present are known as…

Q: Treatment of a new protein with dansyl chloride reveals two (2) dansyl-labelled derivatives of amino…

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Q: Somatostatin is a tetradecapeptide of the hypothalamus that inhibits the release of pituitary growth…

A: The primary structure of somatostatin has to be deduced,

Q: Draw the structural formulas of the following peptides, andshow which bond would be cleaved by…

A: The organic or biological compounds in which the carbon atom is bonded to an amine group (NH2), a…

Q: Explain why, when the guanidino group of arginine is protonated, the double-bonded nitrogen is…

A: Arginine is an amino acid. It contains carboxylic acid and amino group on the right side and the…

Q: draw the primary structure of the peptide DKMMS at pH 7.4 and name this peptide and what chain…

A: Primary structure of a peptide refers to the amino acid sequence in the peptide.

Q: Cleavage of the following peptide with cyanogen bromide would result in the production of smaller…

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Q: Calculate the pH at which the e-amino group of lysine is 25% dissociated.

A: Step : 1             Calculate the pH at which the e-amino group of lysine is 25% dissociated.

Q: Reaction of a polypeptide with carboxypeptidase A releases Met. The polypeptide undergoes partial…

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Q: The pKa of the amino and carboxyl groups on alanine are 9.9 and 2.4, respectively. Under…

A: pKa of amino group=9.9 pKa of carboxyl group=2.4 pH=7.4

Q: Write the mechanism for the reaction of an amino acid with di-tert-butyl dicarbonate.

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Q: Draw the structure for the peptide CF. • You do not have to consider stereochemistry. • You do not…

A: Given peptide, CF C- Cysteine F - Phenylalanine

Q: Arginine and lysine side chains fit into trypsin’s binding pocket . One of these side chains forms a…

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Q: Describe the primary structure ofproteins, and draw the structure of thepeptide bond.

A: Primary constituents of proteins and peptides are amino acids. Amino acids are organic molecules…

Q: If you had a protein X, which is a soluble enzyme found inside the peroxisome, and you wished to…

A: Proteins chain of amino acids which join together to form protein. Proteins are found in the…

Q: What is the isoelectric point for the peptide MNPQR at pH 7? Draw the structure, including the…

A: The mentioned peptide is MNPQR.

Q: which amino acids has a side chains with a conjugate acid form that is neutral?

A: Amino acids are the molecules which containing an amine group, a carboxylic acid group and a side…

Q: Draw the structure of the following amino acid at pH 1 and pH 3. pKa a - COOH 2.19 pKa a - NH2 9.67,…

A: If pH is less than the pKa value of carboxylic acid or NH2 group then, these group would be…

Q: N' HN Where on this amino acid does it attach to a primary sequence of a protein and where is the…

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Q: Why is the amino acid proline not commonly found in alpha-helices or beta-sheets?  In what secondary…

A: The reason for proline not found in α helix or β sheet:It can’t donate an amide hydrogen bond.The…

Q: shows the specificity pockets. The S₁ pocket has a glutamic acid in the bottom, the S₂ pocket is…

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Q: Arginine is an amino acid which has the following pKa values: pK1: 2.17, pK2: = 9.04, pKR = 12.48.…

A: So, the net charge of arginine at pH = 4 will be +1.

Q: what is the overall net charge on the peptide KKSG at pH 7.0?

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Q: What is the major force responsible for the formation of an a-helix in protein secondary structure?…

A: In this question, we will see which force is responsible for making alpha helix in secondary…

Q: Draw three-dimensional representations of the following amino acids.(a) l-phenylalanine

A: The compounds that contain amine group and carboxyl group attached with a side chain usually alkyl…

Q: Why are Guanidins and Amidins such strong bases?

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Q: Determine the oxidation states for each atom indicated in the structure of alanine below.

A: We have to find out the oxidation no of indicated atom

Q: Taking the structure of the amino acids into account, give a comparative discussion of these pK…

A: Amino acids are the biomolecules in which central carbon atom is attached to a carboxylate group,…

Q: The compound shown below is used to fluorescently label proteins: но. но Which of the following…

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Q: Calculate the pH at which the e-amino group of lysine is 25% dissociated. Calculate the pH at which…

A: In order to find the pH at which the ε-amino group of the lysine dissociates we first write done the…

Q: Reaction of the intact peptide with 1-fluoro-2,4-dinitrobenzene followed by hydrolysis creates Ala…

A: 1-fluoro-2,4-dinitrobenzene is Sanger's reagent.

Q: Draw the structure of the following molecule The amino acid phenylalanine at pH 1

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Q: Write the complete structures for the following peptides. Tell whether each peptide is acidic,…

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Q: Decide if the side chains of the following peptides are nonpolar or polar, and label the hydrophobic…

A: Non-polar amino acids are hydrophobic in nature and polar amino acids are hydrophilic in nature. (a)…

Q: Write the complete structures for the following peptides. Tell whether each peptide is acidic,…

A: (a) The structure of peptide formed from methionine and threonine which is known as…

Q: Identify the classification of amine in arginine.

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Q: Explain why site-directed mutagenesis of aspartate to asparagine in the active site of rypsin…

A: Answer - Aspartate - Aspartate is a vitamin-like substance called an amino acid. As a dietary…

Q: Although tryptophan contains a heterocyclic amine, it is considered a neutral aminoacid. Explain why…

A: In tryptophan structure, nitrogen has lone pair of electrons but that electron is involved in…

Q: Define the following terms: a. peptide bond b. Schiff base c. disulfide bridge d. aldimine e.…

A: Since you posted multiple choice question. I will answer for the first three. (a) peptide bond -…

Q: Explain why, when the guanidino group of arginine is protonated, the double-bonded nitrogen is the…

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Q: His-Met-Asp-Tyr-Phe-Ser within this peptide, which amino acid residue is the most hydrophobic and…

A: Hydrophobic amino acids are those with side-chains that do not like to reside in an aqueous…

Spectroanalytical Methods

Spectroanalytical methods measure the wavelength and intensity of radiations that are either emitted or absorbed by a molecular or atomic species. These methods are useful for evaluating the electronic or atomic arrangement of the molecules of a given analyte.