**Title: Predominant Forms of Tyrosine at Different pH Levels****Introduction:**Understanding the predominant forms of amino acids at various pH levels is essential for studying biochemical processes. Below are the structures of the amino acid tyrosine at different pH values: 3.5 and 13.0.**At pH 3.5:**- **Structure:** - The amino group (-NH₃⁺) is protonated. - The carboxyl group is in its non-ionized form (-COOH). - The aromatic ring (phenol group) remains neutral. - Charge: The structure exhibits an overall positive charge due to the protonated amino group.**Diagram Explanation:**- The structure consists of a central carbon atom bonded to: - An amino group (NH₃⁺ to the left). - A carboxyl group (COOH above). - A side chain featuring a benzene ring with an attached hydroxyl group (OH) at the para position.**At pH 13.0:**- **Structure:** - The amino group is in its deprotonated form (-NH₂). - The carboxyl group is in its ionized form (-COO⁻). - The phenolic hydroxyl group is deprotonated. - Charge: The structure has an overall negative charge due to the deprotonated carboxyl and phenolic groups.**Diagram Explanation:**- The structure is similar to the one at pH 3.5 with the following differences: - The amino group is represented as NH₂. - The carboxylate group is shown as COO⁻. - The phenolic OH group is depicted as O⁻, indicating deprotonation.**Conclusion:**These illustrations of tyrosine at pH 3.5 and 13.0 demonstrate how the ionization states of functional groups change with pH, reflecting their chemical behavior in different environments. Understanding these changes is crucial in biochemistry and molecular biology applications.

Answered: Image /qna-images/answer/46f2e7ed-f332-4725-a92b-30f9650c16c3.jpg

Modify the structures (if necessary) to show the predominant form of the amino acid tyrosine at each pH. Be sure to include the proper number of hydrogen atoms on heteroatoms and the correct formal charges on atoms.

Modify the structures (if necessary) to show the predominant form of the amino acid tyrosine at each pH. Be sure to include the proper number of hydrogen atoms on heteroatoms and the correct formal charges on atoms.

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Related questions

Q: Write the structural formula (flat projection) of the dipeptide glycyl-phenylalanine (Glycine is the…

A: When the OH group of one amino acid and H of amine group of another amino acid condensed to give a…

Q: Draw a structural formula for the major ionic form of the amino acid shown below when in aqueous…

Q: An unknown acetylenic amino acid obtained from the seed of a tropical fruit has the molecular…

A: The catalytic hydrogenation over platinum is a process of the addition of hydrogen molecules across…

Q: Name the amino acids you would need to put together this peptide: CH-NH C-CH2-NH -C-CH-NH3 CH2 HO…

Q: All amino acids have two ionizable functional groups: an α‑amino group (average p?a of 9.4) and an…

A: The ionization of Aspartic acid according to the question is shown in the figure:

Q: Write the structure for the protein Pro-Asn-Tyr-Cys at pH 7.0.

A: Amino acid: An amino acid is an organic molecule and it consists of amine group (NH2), acidic…

Q: Order the following types of bonding from strongest (=1) to weakest (=5) in a typical biochemical…

A: Rank the various types of bonds in a biochemical system:

Q: Draw the predominant form of this amino acid at pH = 12.

A: Calculate the isoelectric point (pl) for the given amino acid At pI the amino acid exist as…

Q: Identify the following amino acid in aqueous form (at pH = 7.0): (COO)–CH(NH3)–CH(OH)–CH3 A.…

A: Acidic and basic amino acid did not have equal number of acid and amine groups . For neutral amino…

Q: Consider an amino acid with the following pKa values: pKa1 = 2.71 and pK, = 9.31 At what pH value in…

A: Amino acids are amphoteric in nature due to the presence their ionizable α-amino and α-carboxylic…

Q: QUESTION 19 Briefly explain why there are + and - charges in the amino acid structures in the table…

Q: given a solution of alanine at pH 9.00, draw the structure of the species present in appreciable…

A: The given amino acid is alanine. pH of the given alanine solution = 9.00The Henderson-Hasselbalch…

Q: Consider this amino acid shown here at pH 7.0 (the isoelectric point for this amino acid is 9.7).…

Q: Omplete the electron-dot structure of phenylalanine, showing all lone-pair electrons. • Include all…

Q: An amino acid is usually more soluble in aqueous solvent at pH extremes than it is at a pH near the…

A: We know, aqueous solvents are usually polar in nature and polar solvents dissolve polar compounds…

Q: Identify the amino group present in the given amino acid. COO™ H₂N-CH | CH₂OH Serine

A: Zwitter ion form of amino acid Is given.Zwitter ion is one which have both ions (+ ,-)positive as…

Q: What amino acid is found at this position: 148 of 4ALD? Explain why this position in your protein is…

A: 4 ALD also known as Human muscle protein. ( FRUCTOSE 1,6 - BIPHOSPHATE ALDOLASE) It has a sequence…

Q: Alanine, shown below, is an example of a(n) [Select] amino acid and would most likely be found on…

A: Alanine is an aliphatic alpha-amino acid used in the biosynthesis of protein. the IUPAC name of…

Q: d) Amino acids show both acidic and basic properties. Write equations to illustrate the reactions…

A: The question is based on concept of acid- base reaction. we have to show reaction of amino acid…

Q: 13.2) Draw the line bond structure for the general form of an amino acid using "R" to represent the…

A: Here we have to draw line structure of predominant form of amino acid at physiolgical pH = 7.4

Q: ogen pept is rigid, take place about the N-Co and the Co-C bonds in a protein (Co is the a carbon…

Q: Calculate the molecular weight of a small protein if 5.90 g sample of this protein is dissolved in…

A: P = CRTWhere, P = osmotic pressure in atm; R = 0.0821 L atm mol-1 K-1, T = temperature in K

Q: НОНН С. H,N-C-C-N-C-C-OH НОСН CH;CHCH, HOH H O TITT I H,N-C-C-N-C-C-OH d. H.NCH.CH.CH.СHН H

A: Amino acids are building blocks of proteins. they're concerned with many chemical and biological…

Q: The use of salt bridges or hydrophobic interactions (or pockets) to stabilize interactions between…

A: Proteins are chain of polypeptide, and tertiary structure of protein is three-dimensional structure…

Q: Draw a structural formula for the major ionic form of the amino acid shown below when in aqueous…

Q: Match the following amino acids with their chemical properties - VA - VB с D A VG O || H CH CH3 CH3…

A: Amino acids contain both amine and carboxylic acid functional groups.. In alpha amino acids the…

Q: Considering the peptide structure on the image, label N-terminus and C-terminus, circle each of the…

A: Given that, a structure of a peptide. We have to assign the N-terminus and C-terminus. Also we have…

Concept explainers

Ionic Equilibrium

Chemical equilibrium and ionic equilibrium are two major concepts in chemistry. Ionic equilibrium deals with the equilibrium involved in an ionization process while chemical equilibrium deals with the equilibrium during a chemical change. Ionic equilibrium is established between the ions and unionized species in a system. Understanding the concept of ionic equilibrium is very important to answer the questions related to certain chemical reactions in chemistry.

Arrhenius Acid

Arrhenius acid act as a good electrolyte as it dissociates to its respective ions in the aqueous solutions. Keeping it similar to the general acid properties, Arrhenius acid also neutralizes bases and turns litmus paper into red.

Bronsted Lowry Base In Inorganic Chemistry

Bronsted-Lowry base in inorganic chemistry is any chemical substance that can accept a proton from the other chemical substance it is reacting with.

Question

**Title: Predominant Forms of Tyrosine at Different pH Levels**

**Introduction:**
Understanding the predominant forms of amino acids at various pH levels is essential for studying biochemical processes. Below are the structures of the amino acid tyrosine at different pH values: 3.5 and 13.0.

**At pH 3.5:**

- **Structure:**
- The amino group (-NH₃⁺) is protonated.
- The carboxyl group is in its non-ionized form (-COOH).
- The aromatic ring (phenol group) remains neutral.
- Charge: The structure exhibits an overall positive charge due to the protonated amino group.

**Diagram Explanation:**
- The structure consists of a central carbon atom bonded to:
- An amino group (NH₃⁺ to the left).
- A carboxyl group (COOH above).
- A side chain featuring a benzene ring with an attached hydroxyl group (OH) at the para position.

**At pH 13.0:**

- **Structure:**
- The amino group is in its deprotonated form (-NH₂).
- The carboxyl group is in its ionized form (-COO⁻).
- The phenolic hydroxyl group is deprotonated.
- Charge: The structure has an overall negative charge due to the deprotonated carboxyl and phenolic groups.

**Diagram Explanation:**
- The structure is similar to the one at pH 3.5 with the following differences:
- The amino group is represented as NH₂.
- The carboxylate group is shown as COO⁻.
- The phenolic OH group is depicted as O⁻, indicating deprotonation.

**Conclusion:**
These illustrations of tyrosine at pH 3.5 and 13.0 demonstrate how the ionization states of functional groups change with pH, reflecting their chemical behavior in different environments. Understanding these changes is crucial in biochemistry and molecular biology applications.

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

This is a popular solution!

SEE SOLUTION Check out a sample Q&A here

Step 1: Write the general conditions for assigning charge of amino acid

VIEW

Step 2: Draw the correct structures at pH 3.5 and pH 13.0

VIEW

Solution

VIEW

Trending now

This is a popular solution!

Step by step

Solved in 3 steps with 3 images

SEE SOLUTION Check out a sample Q&A here

Knowledge Booster

Learn more about

Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.

Similar questions

Consider a "tripeptide" with the following features (at pH = 10.8) • The N-terminal amino acid is leucine • The middle amino acid is aspartate • The C-terminal amino acid is lysine i. What is the 1-letter symbol for each of these amino acids il. Calculate the net charge of the predominant ionic state of this tripeptide at pH 10.8. Show work.
Am I correct? Please help
Now let us look at a real amino acid, alanine. Fill in the chart below for each ionizable group. You need only the relationship discussed in the pdf posted and the numbers posted below. The next 6 questions will ask for the numbers you calculated for each of the letters below. pH when Average charge of group Group Ka pKa [A]/[HA] = 1 when pH = pK alpha-COOH ~10-2 A C alpha-NH3* ~10-9 В
How is this wrong?
Researchers discover a new amino acid. Its R-group exclusively has hydrogen and carbon atoms. What behavior will this amino acid show? O Relative to the amino acids found in organisms, its interactions with water will be very high. It is hydrophilic. Relative to the amino acids found in organisms, its interactions with water will be intermediate. It is hydrophobic.
Identify the part of a generic amino acid that reacts with base and the part that reacts with acid. Briefly explain your answer.Hint: Draw Lewis structures for ammonia (NH 3) and acetic acid (CH 3COOH).
write structural formulas for all the ionic forms of glutamic acid, and calculate its isoelectric ph.
HW7 #14
All amino acids have two ionizable functional groups: an α‑amino group (average pKa of 9.4) and an α‑carboxylic acid group (average pKa of 2.2). Aspartic acid has an ionizable side chain (R group) with a pKa of about 3.8. One of the possible ionization states of aspartic acid is shown in the image. At what pH would the structure be the predominant ionization state? Consider the ionization state of all three of the functional groups.
Please don't provide handwritten solution .....
Q3- We wish to synthesize all possible dipeptides containing the amino acids tyrosine, lysine, phenylalanine, and leucine. Identify the number of possible dipeptides and explain how we would carry this out using combinatorial techniques.