17.15 The structure of aspartic acid (pl = 2.8) is shown below. Draw the structure of aspartic acid at pH= 1, 2.8, 7 and 10. O rod opg H₂N-CH-C-OH pK₂2 = 9.6 91 CH₂ C1O SW as not bed-pka1 = 1.88 bspK₂3 = 3.65 OH pka3 sbitqoq e

Q: calculate the % yield of preparation of 2-aminobenzoic acid: mass of phthaliamide = 2.95g mass of…

A: In the  question two mass of 2-aminobenzoic acid is given. Hence, the individual percent yield is…

Q: Hydroxychloroquine is a weak Bronsted base.

A: According to Arrhenius' concept, an acid gives H+ ions in its aqueous solution and a base gives OH-…

Q: Glutamic acid is a naturally occuring a-amino acid that contains a carboxy group in its R group side…

A: a. At pH=1, there is a highly acidic medium, the amino group gains a proton and the positive form of…

Q: Glutamic acid as the following structure at physiological pH. Identify the structure of Glutamic…

A: Glutamic acid is the compound that belongs to an amino acid. Amino acids are the compounds…

Q: What is the pI of the amino acid show below?

A: PI is the isoelectric point where there is no net formal charge. Given : pKa1 = 2.18 pKa2 = 8.95…

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

A: The objective of this question is to find the pH of histidine.

Q: what are the lewis structures of these: H3PO4 SO42- Palmitic acid (in pH 7.4) Glycerol Water…

A: Lewis structure are drawn by making dots on the symbol of atom the number of dots are equal to their…

Q: 8. The following proteins represent a wide range of molecular weights and isoelectric points. Mr is…

A:

Q: Phenolphthalein has a pKa of 9.7. It is colorless in its acid form and pink in its basic form. For…

A:

Q: 4. Write out the 1° structure for the following polypeptide: Ο Η ОН H₂N-CH-C-N-CH-C-N-CH-COO T CH-OH…

A:

Q: Find the pH of 0.1 M of the different form of histidine species. (See image attached)  b) What is…

A: Histidine is an amino acid

Q: Which is the most important factor in stabilizing alpha helix secondary structure of proteins? salt…

A: Proteins are large polymers of amino acids. The structure of a protein is determined at different…

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: Make

A: According to the question, molecule C4H11N5 was the side chain of an amino acid, in a protein, we…

Q: what is the overall charge on the peptide : Pro- Glu-Tyr-Gln-Arg at pH=11

A: A polypeptide or simply peptide is an entity that contains amino acids bonded to each other by…

Q: If the pl for asparagine is 5.43, draw the structure at a pH of 9.5?

A: The pl for asparagine = 5.43 pH = 9.5

Q: 14. ¿Qué porcentaje de glicinamida, ⒸH₂NCH,CONH, (pK 8.20) no está protonado a a) pH = 7.5, b) pH =…

A: Given in following question

Q: For aspartic acid, the pka's of the a-COOH and a-NH3* are 2.1 and 9.8, respectively, whereas the pKa…

A: When pH is greater than pKa then depronated form.  When pH is less than pKa then protonated form.…

Q: H₂N- C-C-OH _______ CH₂ CH₂ CH3 Give the pK₂ value for the a-amino group of methionine. An answer…

A: Given the structure of methionine in its +1 charge state. In the +1 charge state, methionine has…

Q: Show how L-Serine can act as buffer when you add H3O+ or OH- ions Write equations to show this.

A:

Q: Draw the structure of alanine in a solution at pH = 0 2. Draw the structure of alanine in a…

A: Amino acids are  compounds that contain amino and carboxylate functional groups, along with a side…

Q: Describe the cyclization reaction for pyranoses & furanoses: why it occurs, how it creates two…

A:

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…

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.