BackStudy Guide: Biological Molecules (General Biology)
Study Guide - Smart Notes
Tailored notes based on your materials, expanded with key definitions, examples, and context.
Biological Molecules
Introduction
Biological molecules, also known as biomolecules, are essential compounds that form the structure and function of all living organisms. This chapter focuses on the chemistry of organic molecules, their diversity, and their roles in biological systems.
Organic Molecules
Definition and Characteristics
Organic molecules are compounds primarily composed of carbon atoms bonded with hydrogen, oxygen, nitrogen, and other elements.
Carbon can form four covalent bonds, allowing for a wide variety of molecular shapes and sizes, including chains, rings, and branched structures.
This versatility enables the formation of complex molecules necessary for life.
Significance: The diversity of carbon-based molecules underlies the complexity and adaptability of living organisms.
Functional Groups
Role in Biomolecules
Functional groups are specific groups of atoms within molecules that determine the chemical properties and reactions of those molecules.
Common functional groups in biology include amino (-NH2), carboxyl (-COOH), hydroxyl (-OH), and phosphate (-PO4).
For example, amino acids contain both amino and carboxyl groups; ATP contains phosphate groups.
Polymers and Monomers
Formation and Breakdown
Polymers are large molecules made by joining many smaller units called monomers.
Dehydration synthesis (condensation reaction): Monomers are joined by covalent bonds through the removal of a water molecule.
Hydrolysis: Polymers are broken down into monomers by the addition of water.
Example: The formation of a disaccharide from two monosaccharides by dehydration synthesis:
Major Groups of Biomolecules
Overview and Characteristics
There are four major classes of large biomolecules: carbohydrates, lipids, proteins, and nucleic acids.
Each group has distinct structures, monomers, and functions in organisms.
BioMolecule Group | Uses in Organisms | Monomers or Common Subunits | Reaction to Water (Hydrophobic/Hydrophilic) |
|---|---|---|---|
Carbohydrates | Energy storage, structural support | Monosaccharides (e.g., glucose) | Hydrophilic |
Lipids | Energy storage, membrane structure, signaling | Glycerol and fatty acids | Hydrophobic |
Proteins | Catalysis, structure, transport, signaling | Amino acids | Varies (depends on R group) |
Nucleic Acids | Genetic information storage and transfer | Nucleotides | Hydrophilic |
Carbohydrates
Monosaccharides and Polysaccharides
Monosaccharides are simple sugars with a general formula of (CH2O)n.
The most biologically important monosaccharide is glucose (C6H12O6).
Disaccharides are formed by joining two monosaccharides via dehydration synthesis.
Polysaccharides are long chains of monosaccharides. Four key polysaccharides are:
Starch (energy storage in plants)
Glycogen (energy storage in animals)
Cellulose (structural support in plant cell walls)
Chitin (structural support in fungi and arthropods)
All are polymers of glucose but differ in the type of glycosidic bonds and branching, leading to different properties.
Lipids
Characteristics and Types
Lipids are a diverse group of hydrophobic molecules, grouped together by their insolubility in water.
Major types include triacylglycerols (fats and oils) and phospholipids (major component of cell membranes).
Triacylglycerol consists of three fatty acids linked to a glycerol molecule.
Phospholipids have two fatty acids and a phosphate group attached to glycerol, giving them both hydrophobic and hydrophilic regions.
Saturated fats have no double bonds between carbon atoms; unsaturated fats have one or more double bonds.
Saturated fats are typically solid at room temperature (common in animals), while unsaturated fats are liquid (common in plants).
Proteins
Structure and Function
Proteins perform a wide variety of functions, including catalysis (enzymes), structural support, transport, and signaling.
The diversity of protein function is due to the variety of amino acids (20 different types), each with a unique R group.
Amino acids are the monomers of proteins, linked by peptide bonds (formed by dehydration synthesis).
Each amino acid has a central carbon, an amino group, a carboxyl group, a hydrogen atom, and an R group (side chain).
The properties of the R group determine the behavior of the amino acid in a protein (e.g., hydrophobic, hydrophilic, acidic, basic).
Protein Structure
Proteins have four levels of structure:
Primary structure: Sequence of amino acids.
Secondary structure: Local folding (e.g., alpha helices, beta sheets) stabilized by hydrogen bonds.
Tertiary structure: Overall 3D shape, stabilized by interactions among R groups (hydrogen bonds, ionic bonds, disulfide bridges, hydrophobic interactions).
Quaternary structure: Association of multiple polypeptide chains.
Denaturation disrupts secondary, tertiary, and quaternary structures, often rendering the protein nonfunctional. Causes include heat, pH changes, and chemicals. Denaturation is sometimes reversible, but often is not.
Nucleic Acids
Basic Information
Nucleic acids (DNA and RNA) store and transmit genetic information.
The monomers of nucleic acids are nucleotides.
Further details on nucleic acids will be covered in later chapters.
Additional info: Some explanations and examples have been expanded for clarity and completeness, as the original notes were in outline form.