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Chemistry of Life: Macromolecules and Chemical Bonds in Anatomy & Physiology

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Chemistry of Life and Macromolecules

Introduction

This section explores the foundational chemistry concepts essential for understanding Anatomy & Physiology, focusing on chemical bonds, chemical reactions, and the structure and function of organic macromolecules such as carbohydrates, lipids, proteins, and nucleic acids.

Chemical Bonds and Reactions

Types of Chemical Bonds

  • Ionic Bonds: Formed when electrons are transferred from a metal to a non-metal, resulting in oppositely charged ions that attract each other. Example: NaCl (table salt).

  • Covalent Bonds: Formed when atoms share electrons. These are stronger than ionic bonds and can be:

    • Non-polar Covalent Bonds: Electrons are shared equally (e.g., O2, CO2).

    • Polar Covalent Bonds: Electrons are shared unequally, creating partial charges (e.g., H2O).

  • Hydrogen Bonds: Weak attractions between a partially positive hydrogen atom and a partially negative atom (usually oxygen or nitrogen) in another molecule. These are not true bonds but are crucial for the properties of water and biological molecules.

Hydrogen bonds between water molecules

Chemical Reactions

  • Reactants: Substances that enter into a chemical reaction.

  • Products: Substances produced by a chemical reaction.

  • Synthesis (Anabolic) Reactions: Two or more reactants combine to form a larger product. Example:

  • Decomposition (Catabolic) Reactions: A reactant breaks down into smaller products. Example:

Enzymes

  • Enzymes: Biological catalysts, mostly proteins, that speed up chemical reactions by lowering activation energy. They are essential for metabolism and cellular function.

Organic Macromolecules

Monomers and Polymers

  • Monomers: Small, single subunits that can join together to form larger molecules.

  • Polymers: Large molecules made by linking monomers together.

  • Dehydration Synthesis: Chemical reaction that joins monomers by removing a water molecule. Products: polymer + H2O

  • Hydrolysis: Chemical reaction that breaks polymers into monomers using water as a reactant. Products: monomers

Carbohydrates

Structure and Function

  • Main source of energy for cells (glucose is converted to ATP).

  • Form glycoproteins and glycolipids in cell membranes.

Types of Carbohydrates

  • Monosaccharides: Simple sugars (e.g., glucose, fructose, galactose).

  • Disaccharides: Two monosaccharides joined by a glycosidic bond (e.g., sucrose, maltose, lactose).

  • Polysaccharides: Long chains of monosaccharides (e.g., starch in plants, glycogen in animals).

Structures of pentose and hexose sugarsFormation of disaccharides by dehydration synthesisStructure of glycogen, a polysaccharide

Lipids

Structure and Function

  • Composed mainly of nonpolar hydrocarbons; hydrophobic (insoluble in water).

  • Major types: triglycerides, phospholipids, steroids.

Fatty Acids

  • Saturated Fatty Acids: No double bonds; solid at room temperature.

  • Unsaturated Fatty Acids: One or more double bonds; liquid at room temperature.

    • Monounsaturated: One double bond.

    • Polyunsaturated: Two or more double bonds (e.g., omega-3 fatty acids).

Saturated fatty acid structureMonounsaturated fatty acid structurePolyunsaturated fatty acid structure

Triglycerides

  • Formed by joining three fatty acids to a glycerol molecule via dehydration synthesis.

  • Functions: energy storage, insulation, protection of organs, absorption of fat-soluble vitamins.

Formation of triglycerides

Phospholipids

  • Composed of a glycerol backbone, two fatty acids (hydrophobic), and a phosphate group (hydrophilic).

  • Main component of cell membranes; act as emulsifiers.

Phospholipid structure

Steroids

  • Structure: Four fused hydrocarbon rings.

  • Functions: Components of cell membranes (cholesterol), hormones, bile acids.

Steroid and cholesterol structure

Proteins

Structure and Function

  • Functions: Enzymes, structural support, transport, signaling, immune response, acid-base balance.

Amino Acids

  • Monomers of proteins; each contains a central carbon, hydrogen, amino group, carboxyl group, and variable R group.

Amino acid structure

Peptide Bonds and Protein Structure

  • Peptide bonds form between amino acids via dehydration synthesis.

  • Proteins have four levels of structure:

    • Primary: Sequence of amino acids.

    • Secondary: Alpha helices and beta sheets formed by hydrogen bonding.

    • Tertiary: Overall 3D shape of a single polypeptide.

    • Quaternary: Assembly of multiple polypeptide chains.

Peptide bond formation and dipeptide structureProtein secondary structure: alpha helix and beta sheetProtein tertiary and quaternary structureFibrous and globular protein structures

Nucleic Acids and Nucleotides

Nucleotides

  • Monomers of nucleic acids; each consists of a phosphate group, a pentose sugar (ribose or deoxyribose), and a nitrogenous base (adenine, guanine, cytosine, thymine, or uracil).

Nucleotide structure and nitrogenous bases

DNA and RNA

  • DNA: Double-stranded, stores genetic information, uses complementary base pairing, held together by phosphodiester and hydrogen bonds.

  • RNA: Single-stranded, involved in protein synthesis and gene regulation, contains uracil instead of thymine.

DNA and RNA structureDNA and RNA structure (alternate view)

Adenosine Triphosphate (ATP)

  • Structure: Ribose sugar, adenine base, and three phosphate groups.

  • Function: Main energy currency of the cell; energy is stored in the high-energy phosphate bonds and released during hydrolysis.

ATP structureATP/ADP energy cycle

Summary Table: Major Macromolecules

Macromolecule

Monomer

Bond Type

Main Functions

Carbohydrates

Monosaccharides

Glycosidic

Energy, cell recognition

Lipids

Fatty acids, glycerol

Ester

Energy storage, membranes, hormones

Proteins

Amino acids

Peptide

Enzymes, structure, signaling

Nucleic Acids

Nucleotides

Phosphodiester

Genetic information, energy (ATP)

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