The electrospray ionization mass spectrum of the tripeptide Ala-Met-Thr shows peaks of mono-protonation and di-protonation of the tripeptide. At what values of m/z would these peals be expected? Briefly explain and show your workings.

Q: Use the values provided below to calculate the predicted isoelectric point, pl, value for aspartame…

A: Isoelectric point:  Isoelectric point of a amino acid is the pH at which amino acid has a neutral…

Q: Look up the pKa values for trimethylamine, dimethylamine, ethylamine, and ammonia. Predict the order…

A: Ion exchange chromatography is the process by which a mixture of similar charged ions can be…

Q: Look up the pKa values for trimethylamine, dimethylamine, methylamine, and ammonia. Predict the…

A: pKb tells about the basicity of any organic base. Higher the pKb value, lower would be the basicity.

Q: True or false and why is false 8   Structures produced by X-ray diffraction are as good as the…

A:

Q: 4b) Canavanine is closely related to arginine, and like arginine its side group has a +1 charge when…

A: Canavanine has a similar structure of Arginine.  Hence Canavanine has 3 groups that can be…

Q: Estimate the pI of a dipeptide Cys-Asp assuming that the pKa values for αα-NH3+, αα-COOH, side chain…

A: The question is based on the concept of peptides. we have to identify the isoelectric point of given…

Q: Biotin has a single ionizable group with a pKa of 4.5. If you dissolved biotin in an aqueous…

A: The question is based on the concept of biomolecules. We have to account for the dissociation…

Q: ted elution order of lysine, aspartic acid, and phenylalanine? ning

A: The order of elution depends on the side chains of the amino acids. The side chains will either lose…

Q: If a particular 150 amino acid polypeptide is known to sample 4 preferred states as it folds into…

A:

Q: A protein consists of two types of peptide chains (A and B) with an unknown stoichiometry (AxBy).…

A: Given that: peak area of A = 500,000 peak area of B = 100,000 molecular mass of A =  25,000…

Q: 2) Part of the 'H NMR spectrum for a dipeptide recorded in D₂O is shown below. The signal for the CH…

A: When molecules are placed in a strong magnetic field, the nuclei of some atoms will begin to behave…

Q: The electrophoresis of a sample containing 2-amino-4-methylpentanoic acid. (pKa of a-COOH = 2.2, pKa…

A:

Q: (II) Draw all the ionic forms of the amino acid and determine the predominant structure at pH 8.2.

A: Structure of amino acids

Q: In what order would histidine, serine, aspartate, and valine be eluted with a buffer of pH 4 from a…

A: The order in which the following would the amino acids will be eluted with the buffer of pH 4 from a…

Q: Without performing a calculation, predict whether the standard entropies of the following reactions…

A: Entropy is the measure of randomness in the reaction. If the randomness increases the entropy…

Q: The negative ion mode electrospray ionization (ESI) mass spectrum of an oligonucleotide shows peaks…

A:

Q: Draw the most prominent ionization state for phenylalanine (pKa for acidic hydrogens shown below) at…

A: Amino acids contain carboxylic acid and an amine functional group on the same carbon atom. Amino…

Q: Show the condensation reactions that result in the formation of the tetrapeptide Asp-Gly-Ser- Gln.…

A: Given: Asp, Gly, Ser, GIn To determine: 1) The condensation reactions that result in the formation…

Q: The pKa values of an amino acid are the following: pK1 = 2.18;  pK2 = 8.95;  pK3 = 10.53, what is…

A: Tha pKa values indicates ;  pK1 = 2.18 ( this is the pKa of acidic group)  pK2 and pK3 are the pKa…

Q: Electrophoresis of a mixture of lysine, histidine, and cysteine is carried out at pH 7.64. Describe…

A: The pH at which amino acid is neutral, or in other words have both negative and positive charge, is…

Q: Determine the buffer capacity of Alanine and Histidine at pH 2.0 and 6.0 respectively and discuss…

A: For the alanine, the value for pKa is 2.34. Now the salt to amino acid ratio to achieve the pH of…

Q: Most of the ultraviolet absorption of proteins at 280 nm is due to their content of a. Glutamate b.…

A:

Q: Draw a structure for a peptide that gives Ala, Leu & Val on hydrolysis and fails to react with…

A: Amino Acids  Amino acids are very essential for our body and facilitate numerous biological…

Q: The amino acid histidine has ionizable groups with pKa values of 1.8, 6.0, and 9.2, as shown. COOH…

A: Molarity of Histidine solution = 0.11 MThe volume of Histidine solution taken = 80 mLpH of Histidine…

Q: b=3.50 = 3.50 3.30 d=335 나50. 7 3 2 1. 17-706 ppm 00

A: Glycerol is hygroscopic in nature due to extensive hydrogen bonding

Q: Rank the migration rate of the following amino acids in ascending order towards  the cathode when…

A: PI stands for isoelectric point. If pH is less than isoelectric point then amino acid will move…

Q: Asparagine and glutamine residues in proteins are deamidated in an aqueous solution to yield…

A: Deamidation is the conversion of amide group to another functional group. Side chain of amino acid…

Q: 2. The heptapeptide ALA-TYR-LYS-ASP-MET-CYS--SER was treated with trypsin and then with cyanogen…

A: In the anionic exchanger column, the pH to which the anion exchanger resin is adjusted, if the pI of…

Q: Calculate the pI of arginine. Give your answer to two decimal places. pI =

A: pH at which the net charge on amino acid is zero is called Isoelectric point (pI).   pI value of…

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.