Nitrogen Containing Organic Compounds

SOME CARBON-NITROGEN COMPOUNDS OF BIOLOGICAL IMPORTANCE

  • Nitrogen-containing organic compounds play crucial roles in biological processes
  • These compounds are essential for the structure and function of living organisms
  • Some important carbon-nitrogen compounds include:
  • Amino acids
  • Proteins
  • Nucleic acids
  • Enzymes
  • Hormones
  • Let’s explore each of these compounds in detail.

Amino Acids

  • Amino acids are the building blocks of proteins
  • They contain a carboxyl group (-COOH) and an amino group (-NH2) attached to the same carbon atom
  • There are 20 naturally occurring amino acids
  • Examples of amino acids include alanine, glycine, and valine
  • Amino acids can act as acids or bases depending on the pH of the solution

Proteins

  • Proteins are large, complex molecules made up of amino acids
  • They have various functions in the body, including structural support, enzymatic activity, and transportation of molecules
  • The primary structure of a protein is determined by the sequence of amino acids
  • Examples of proteins include hemoglobin, insulin, and collagen
  • Proteins fold into a specific three-dimensional structure to carry out their functions

Nucleic Acids

  • Nucleic acids are macromolecules that store and transmit genetic information
  • There are two types of nucleic acids: DNA (deoxyribonucleic acid) and RNA (ribonucleic acid)
  • Nucleic acids are composed of nucleotides, which consist of a sugar, a phosphate group, and a nitrogenous base
  • Examples of nucleic acids include DNA, RNA, and ATP (adenosine triphosphate)
  • Nucleic acids play a crucial role in protein synthesis and inheritance of traits

Enzymes

  • Enzymes are biological catalysts that speed up chemical reactions in living organisms
  • They are made up of proteins and often require cofactors or coenzymes to function properly
  • Enzymes are highly specific and can catalyze a wide range of reactions
  • Examples of enzymes include amylase, pepsin, and DNA polymerase
  • Enzymes play a vital role in metabolism, digestion, and regulation of cellular processes

Hormones

  • Hormones are chemical messengers that regulate various physiological processes in the body
  • They are produced by endocrine glands and travel through the bloodstream to target cells
  • Hormones can be proteins, peptides, or steroid derivatives
  • Examples of hormones include insulin, thyroxine, and adrenaline
  • Hormones control growth, metabolism, reproduction, and other important functions in the body

Summary

  • Carbon-nitrogen compounds of biological importance are essential for living organisms
  • Amino acids are the building blocks of proteins
  • Proteins have various functions and fold into a specific structure
  • Nucleic acids store and transmit genetic information
  • Enzymes are biological catalysts that speed up chemical reactions
  • Hormones are chemical messengers that regulate physiological processes
  • Understanding these compounds is essential in studying the chemistry of life.

Amino Acids - Structure and Classification

  • Amino acids contain an amino group (-NH2) and a carboxyl group (-COOH)
  • The central carbon atom is called the alpha carbon
  • The side chain (R group) determines the properties of the amino acid
  • Amino acids can be classified as:
    • Nonpolar (hydrophobic)
    • Polar (hydrophilic)
    • Charged (acidic or basic)

Nonpolar Amino Acids

  • Nonpolar amino acids have hydrophobic side chains
  • Examples include alanine, glycine, and valine
  • These amino acids tend to cluster together in the interior of proteins
  • They do not readily interact with water

Polar Amino Acids

  • Polar amino acids have hydrophilic side chains
  • Examples include serine, cysteine, and glutamine
  • These amino acids readily interact with water
  • They can form hydrogen bonds with other polar molecules

Charged Amino Acids: Acidic

  • Acidic amino acids have a negatively charged side chain at physiological pH
  • Examples include aspartic acid and glutamic acid
  • The side chain can dissociate to release a hydrogen ion (H+)
  • These amino acids are negatively charged in solution

Charged Amino Acids: Basic

  • Basic amino acids have a positively charged side chain at physiological pH
  • Examples include lysine, arginine, and histidine
  • The side chain can accept a hydrogen ion (H+)
  • These amino acids are positively charged in solution

Proteins - Structure and Functions

  • Proteins are polymers of amino acids linked by peptide bonds
  • The primary structure is the sequence of amino acids
  • The secondary structure is the local folding of the polypeptide chain
  • The tertiary structure is the three-dimensional conformation of the protein
  • The quaternary structure is the arrangement of multiple protein subunits

Primary Structure of Proteins

  • The primary structure is determined by the sequence of amino acids
  • Each amino acid is linked to the next by a peptide bond
  • The sequence of amino acids is encoded in the DNA

Secondary Structure of Proteins

  • The secondary structure refers to the local folding patterns of the polypeptide chain
  • Two common secondary structures are:
    • Alpha helix: The polypeptide chain forms a helical structure
    • Beta sheet: The polypeptide chain forms an extended zigzag structure

Tertiary Structure of Proteins

  • The tertiary structure is the overall three-dimensional conformation of the protein
  • It is determined by interactions between amino acid side chains
  • Interactions include hydrogen bonding, hydrophobic interactions, and disulfide bonds

Quaternary Structure of Proteins

  • Some proteins consist of multiple subunits
  • The quaternary structure refers to the arrangement of these subunits
  • Interactions between subunits stabilize the overall protein structure

Nucleic Acids - DNA (Deoxyribonucleic Acid)

  • DNA is a double-stranded nucleic acid that stores genetic information
  • It consists of nucleotides, which are composed of a sugar (deoxyribose), a phosphate group, and a nitrogenous base
  • There are four nitrogenous bases in DNA:
    • Adenine (A) pairs with thymine (T)
    • Guanine (G) pairs with cytosine (C)
  • The pairing of bases forms the double helix structure of DNA

Nucleic Acids - RNA (Ribonucleic Acid)

  • RNA is a single-stranded nucleic acid that is involved in protein synthesis
  • It also consists of nucleotides with a sugar (ribose), a phosphate group, and a nitrogenous base
  • There are four nitrogenous bases in RNA:
    • Adenine (A) pairs with uracil (U)
    • Guanine (G) pairs with cytosine (C)
  • RNA plays a crucial role in the translation of genetic information from DNA to protein

Nucleic Acids - ATP (Adenosine Triphosphate)

  • ATP is a nucleotide that functions as an energy carrier in cells
  • It consists of adenosine (adenine + ribose) and three phosphate groups
  • The high-energy bonds between the phosphate groups store and release energy
  • ATP is involved in various cellular processes such as muscle contraction and active transport

Enzymes - Properties and Mechanism

  • Enzymes are highly specific catalysts that increase the rate of chemical reactions
  • They lower the activation energy required for a reaction to occur
  • Enzymes are not consumed in the reaction and can be reused
  • Enzymes are specific to a particular substrate, and the active site binds to the substrate
  • Enzymes can undergo conformational changes to promote the reaction

Enzyme Substrate Complex

  • The enzyme binds to the substrate, forming an enzyme-substrate complex
  • The active site of the enzyme is complementary to the substrate
  • The binding of the substrate to the active site allows for specific interactions
  • These interactions facilitate the conversion of the substrate to the product

Factors Affecting Enzyme Activity

  • Enzyme activity can be influenced by several factors, including:
    • Temperature: Enzymes have an optimum temperature for activity
    • pH: Enzymes have an optimum pH for activity
    • Substrate concentration: Increasing substrate concentration can increase enzyme activity, up to a point of saturation
    • Enzyme concentration: Increasing enzyme concentration can increase the rate of reaction

Enzyme Inhibition

  • Enzyme activity can be inhibited by certain molecules or factors
  • Competitive inhibition occurs when a molecule competes with the substrate for the active site
  • Non-competitive inhibition occurs when a molecule binds to a site other than the active site, altering the enzyme’s conformation

Hormones - Types and Functions

  • Hormones are chemical messengers that regulate various physiological processes
  • There are different types of hormones:
    • Peptide hormones: Made up of amino acids, examples include insulin and glucagon
    • Steroid hormones: Derived from cholesterol, examples include estrogen and testosterone
    • Amine hormones: Derived from amino acids, examples include adrenaline and melatonin

Hormonal Regulation

  • Hormones regulate processes such as growth, metabolism, reproduction, and stress response
  • They are secreted by endocrine glands and travel through the bloodstream to target cells or organs
  • Hormones can have both short-term and long-term effects on the body
  • Hormonal imbalances can lead to various disorders and diseases

Feedback Mechanism in Hormonal Regulation

  • Hormonal regulation often involves a feedback mechanism
  • Negative feedback: The response to a stimulus inhibits further hormone release
  • Positive feedback: The response to a stimulus enhances further hormone release
  • Feedback mechanisms help maintain homeostasis and regulate hormone levels