Define the term zwitterion.

Short Answer

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Answer: A zwitterion is a molecule that has both positive and negative charges but is electrically neutral overall. They are commonly found in amino acids and exhibit properties such as high solubility in water, the ability to form strong hydrogen bonds, and a unique buffering capacity. In aqueous solutions, zwitterions can act as either an acid or a base, depending on the pH, helping to maintain the pH of the solution. This makes zwitterions particularly important in the chemistry of biological systems, such as protein structures and function.

Step by step solution

01

Definition of Zwitterion

A zwitterion is a molecule that has both positive and negative charges, but overall, it is electrically neutral. Zwitterions are also known as dipolar ions. They are commonly found in amino acids, the building blocks of proteins.
02

Properties of Zwitterions

Zwitterions have distinctive properties as they contain both positive and negative charges. These properties include high solubility in water, the ability to form strong hydrogen bonds, and a unique buffering capacity.
03

Behavior of Zwitterions in Solutions

In an aqueous solution, zwitterions can act as either an acid or a base depending on the pH of the solution. This ability to function as a buffer helps maintain the pH of the solution. In the case of amino acids, the carboxylic acid group (-COOH) can lose a proton (H+) and become negatively charged, while the amino group (-NH2) can gain a proton and become positively charged, resulting in a zwitterion. The point at which the molecule exists primarily in the zwitterionic form is called the isoelectric point.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Amino Acids
Amino acids are the organic compounds that serve as the building blocks for proteins. Each amino acid consists of a central carbon atom, called the \( \alpha \) carbon, bonded to an amino group (\( -NH_2 \)), a carboxylic acid group (\( -COOH \)), a hydrogen atom, and a unique side chain (called the R group). This structure makes them versatile, as they can join together in long chains to form proteins. The properties of a protein are determined largely by the sequence and characteristics of its amino acids.

Importance for Life

Just consider that every protein in your body, from enzymes to structural components, is made up of amino acids. The human body needs 20 different amino acids to function properly, and while some can be made by the body, others must be obtained from food. Understanding amino acids is not only essential for biochemistry but also for nutrition and health.

Zwitterionic Nature

Crucially, amino acids exhibit zwitterionic properties, which means that in a certain pH range, they can exist with both positively and negatively charged functional groups. This behavior is fundamental to how amino acids interact within cells and forms the basis of protein structures.
Isoelectric Point
The isoelectric point, often abbreviated as pI, is the pH at which an amino acid or other molecule exists as a zwitterion, with no net electric charge. At this specific pH, the molecule does not migrate in an electric field during techniques such as isoelectric focusing. This concept is central to understanding how proteins behave in different environments.

Role in Protein Solubility

Because an amino acid is neutral at its isoelectric point, it is generally least soluble in water and may precipitate out of solution. This principle is frequently exploited in biochemical separation techniques, where adjusting the pH to an amino acid's pI can help in purifying a specific protein.

pI and Protein Function

Enzymes, which are proteins that catalyze biochemical reactions, often have an optimum pH where they are most active. This pH can be near the enzyme's isoelectric point, influencing how the enzyme folds and interacts with other molecules, thus affecting its function.
Buffering Capacity
Buffering capacity refers to a solution's ability to resist changes in pH when acids or bases are added. Buffers are incredibly important in biological systems, as they help maintain a stable environment for enzymes and other cellular functions.

How Buffers Work

A buffer typically consists of a weak acid and its conjugate base or a weak base and its conjugate acid. Within a certain pH range, these compounds work together to either donate or accept protons (\( H^+ \)) in response to pH changes, stabilizing the overall pH level.

Buffers in the Human Body

The human blood, for instance, is a buffer system involving bicarbonate and carbonic acid. This buffering system helps maintain the blood's pH at a narrow range, ensuring that metabolic processes continue to operate efficiently. Similarly, the buffering capacity of amino acids, due to their zwitterionic nature, is essential for preserving the structural integrity and biological activity of proteins.
Dipolar Ions
Dipolar ions, also known as zwitterions, are molecules that possess both a positive and a negative electric charge, yet exhibit no net charge. The term 'dipolar' refers to the presence of two poles of charge within the same molecule.

Dipolar Ions in Amino Acids

Amino acids, at certain pH levels, become ideal examples of dipolar ions. At pH levels around their isoelectric point, they contain both positively charged amino groups and negatively charged carboxylate groups, balancing each other out.

Significance of Dipolar Ions

This dual charge nature influences how amino acids and other zwitterions interact with their surroundings. For example, the dipolar nature influences solubility in water and the molecule's ability to participate in electrostatic interactions. In the context of proteins, these interactions are critical for the protein's three-dimensional structure and, consequently, its function. Understanding the properties of dipolar ions is thus crucial in fields ranging from biochemistry to pharmaceutical design.

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Most popular questions from this chapter

2,4-Dinitrofluorobenzene, very often known as Sanger's reagent after the English chemist Frederick Sanger who popularized its use, reacts selectively with the \(N\)-terminal amino group of a polypeptide chain. Sanger was awarded the 1958 Nobel Prize for chemistry for his work in determining the primary structure of bovine insulin. One of the few persons to be awarded two Nobel Prizes, he also shared the 1980 award in chemistry with American chemists, Paul Berg and Walter Gilbert, for the development of chemical and biological analyses of DNA. Following reaction with 2,4-dinitrofluorobenzene, all amide bonds of the polypeptide chain are hydrolyzed, and the amino acid labeled with a 2,4-dinitrophenyl group is separated by either paper or column chromatography and identified. (a) Write a structural formula for the product formed by treatment of the \(N\)-terminal amino group with Sanger's reagent and propose a mechanism for its formation. (b) When bovine insulin is treated with Sanger's reagent followed by hydrolysis of all peptide bonds, two labeled amino acids are detected: glycine and phenylalanine. What conclusions can be drawn from this information about the primary structure of bovine insulin? (c) Compare and contrast the structural information that can be obtained from use of Sanger's reagent with that from use of the Edman degradation.

How many different tetrapeptides can be made under the following conditions? (a) The tetrapeptide contains one unit each of Asp, Glu, Pro, and Phe. (b) All 20 amino acids can be used, but each only once.

From which amino acid are serotonin and melatonin synthesized, and what types of reactions are involved in their biosynthesis? a. b.

At pH 7.4, with what amino acid side chains can the side chain of lysine form salt linkages?

A tetradecapeptide (14 amino acid residues) gives the following peptide fragments on partial hydrolysis. From this information, deduce the primary structure of this polypeptide. Fragments are grouped according to size. $$ \begin{array}{ll} \hline \text { Pentapeptide Fragments } & \text { Tetrapeptide Fragments } \\ \hline \text { Phe-Val-Asn-Gln-His } & \text { Gln-His-Leu-Gys } \\ \text { His-Leu-Cys-Gly-Ser } & \text { His-Leu-Val-Glu } \\ \text { Gly-Ser-His-Leu-Val } & \text { Leu-Val-Glu-Ala } \\ \hline \end{array} $$

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