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Chapter 31: Problem 145

Match the following Column-I Column-I (a) Glycine Column-II (p) Forms chloroacetic acid with NoCl \(\mathrm{d}\) with \(\mathrm{N}\) (b) Lysine Forms acid wi \(0.4\) hloroacetic h NOCl Neutral (b) \(\mathrm{Ly}\) (c) \(\mathrm{Pr}\) Proline (q) \(\mathrm{Ne}\) inactive \(.\) Optically (r) (d) Glutamic acid (s) Basic (t) Isoelectric point

Short Answer

Expert verified
(a) Glycine - (q), (b) Lysine - (s), (c) Proline - (p), (d) Glutamic acid - (r).

Step by step solution

01

Analyzing Column I

First, let's understand each compound in Column I: (a) Glycine is an amino acid and is the simplest among the 20 standard amino acids. It is neutral and optically inactive. (b) Lysine is a basic amino acid, often used for protein synthesis. (c) Proline is unique among the amino acids due to its cyclic structure, making it active and helping in protein folding. (d) Glutamic acid is an acidic amino acid, often involved in neurotransmission.
02

Analyzing Column II

Next, let's interpret the properties given in Column II: (p) Forms chloroacetic acid with NOCl - This suggests reactivity with nitrosyl chloride leading to a chloro product. (q) Neutral and optically inactive - This corresponds to a compound with no net charge and no optical activity. (r) Isoelectric point - This is the pH at which the compound carries no net electrical charge. (s) Basic - Indicative of a compound that can act as a base, usually accepting protons.
03

Matching Glycine (a)

Glycine is neutral and optically inactive due to the absence of a chiral center, matching with: (a) Glycine - (q) Neutral and optically inactive.
04

Matching Lysine (b)

Lysine has a basic side chain that can accept protons, which corresponds to: (b) Lysine - (s) Basic.
05

Matching Proline (c)

Proline, with its unique cyclic structure, does not fit typical patterns but forms compounds like chloroacetic acid: (c) Proline - (p) Forms chloroacetic acid with NOCl.
06

Matching Glutamic Acid (d)

Glutamic acid has a known isoelectric point since it can donate a proton, and thus: (d) Glutamic acid - (r) Isoelectric point.

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Key Concepts

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

Glycine characteristics
Glycine is a unique amino acid and is considered the simplest of all the amino acids found in proteins. It has a hydrogen atom as its side chain. This simplicity gives glycine distinct chemical properties:
  • Neutrality: Glycine is electrically neutral when in aqueous solution. Its side chain does not carry any charge at physiological pH.
  • Optical inactivity: Glycine is the only amino acid that is not optically active. It lacks a chiral center because it has two hydrogen atoms attached to its alpha carbon. This means it cannot exist in stereoisomers, which are mirror images of each other.
Glycine often acts as an inhibitory neurotransmitter in the central nervous system, highlighting its role beyond protein construction.
Lysine properties
Lysine is one of the essential amino acids, which means our body cannot synthesize it and must be obtained from dietary sources. It is renowned for being basic due to its side chain:
  • Basic nature: Lysine has an amino group on its side chain, making it positively charged at physiological pH. This allows it to interact with acidic molecules and play a crucial role in protein structure and function.
  • Protein synthesis: Lysine is essential for processes such as protein synthesis, enzyme function, and hormone production. Its ability to form hydrogen bonds and ionic interactions stabilizes protein structure.
Overall, lysine's basic properties make it vital for various biological processes, including calcium absorption and immune function.
Proline structure
Proline is well-known for its distinctive cyclic structure. Instead of a typical open chain, its side chain is bonded to the amino group, forming a secondary amine, which imparts unique characteristics:
  • Cyclic structure: The ring structure of proline makes it rigid compared to other amino acids, which significantly affects the way proteins can fold and function.
  • Influence on protein folding: Due to its ring, proline introduces kinks in polypeptide chains and affects the flexibility of the protein backbone. This often limits secondary structure conformations like alpha-helices or beta-sheets, influencing overall protein forms.
Proline's structural role is crucial, particularly in collagen, where it contributes to its stability and architecture.
Glutamic acid function
Glutamic acid, sometimes referred to as glutamate in its ionized form, is integral to numerous physiological functions:
  • Acidic property: It has a carboxylic acid group in its side chain, which gives it an acidic charge at a physiological pH. This feature allows it to donate protons in biochemical pathways.
  • Neurotransmitter role: Glutamic acid is essential in the nervous system as a neurotransmitter. It plays a key role in brain function by exciting neurons and is crucial for cognitive functions like learning and memory.
  • Isoelectric point: The specific pH at which glutamic acid carries no net electrical charge, known as the isoelectric point, is around 3.2, reflecting its highly acidic nature.
Glutamic acid鈥檚 ability to affect nerve signals makes it invaluable for brain health and overall neural communication.

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Most popular questions from this chapter

Hydrolysis of lactose with dilute acid yields (a) equimolar mixture of D-glucose and D-glucose (b) equimolar mixture of D-glucose and Dgalactose (c) equimolar mixture of D-glucose and D-fructose (d) equimolar mixture of D-galactose and Dgala-ctose

Glucose reacts with bromine water to produce (a) glyceraldehyde (b) gluconic acid (c) saccharic acid (d) glutaric acid

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