IB Bio Unit 3

HL Unit 3 Topic List

Form and Function: Molecules

B1.1 Carbohydrates and Lipids

Content Statements:

  • B1.1.1—Chemical properties of a carbon atom allowing for the formation of diverse compounds upon which life is based

  • B1.1.2—Production of macromolecules by condensation reactions that link monomers to form a polymer

  • B1.1.3—Digestion of polymers into monomers by hydrolysis reactions

  • B1.1.4—Form and function of monosaccharides

  • B1.1.5—Polysaccharides as energy storage compounds

  • B1.1.6—Structure of cellulose related to its function as a structural polysaccharide in plants

  • B1.1.7—Role of glycoproteins in cell–cell recognition

  • B1.1.8—Hydrophobic properties of lipids

  • B1.1.9—Formation of triglycerides and phospholipids by condensation reactions

  • B1.1.10—Difference between saturated, monounsaturated and polyunsaturated fatty acids

  • B1.1.11—Triglycerides in adipose tissues for energy storage and thermal insulation

  • B1.1.12—Formation of phospholipid bilayers as a consequence of the hydrophobic and hydrophilic regions

  • B1.1.13—Ability of non-polar steroids to pass through the phospholipid bilayer

Vocabulary and Topics:

  • Carbon

  • Organic chemistry

  • Covalent bond

    • Polar covalent bonds

    • Nonpolar covalent bonds

    • Electronegativity

  • Hydrogen bond

  • Valence electrons

  • Valence

  • Tetravalence

  • Hydrocarbon

  • Functional groups (know how to recognize)

    • Hydroxyl (OH)

    • Carboxyl (COOH)

    • Amino (NH2)

    • Phosphate (PO43-)

  • Macromolecules

  • Metabolism

    • Anabolic

    • Catabolic

    • Condensation

    • Hydrolysis

    • Monomer

    • Polymer

    • Endergonic

    • Exergonic

  • Nucleic Acids

    • Elements: CHONP

    • Nucleotide

    • Polynucleotide

    • Phosphodiester bond

  • Proteins

    • Elements: CHON (sometimes S)

    • Amino acids

    • Polypeptide

    • Peptide bond

  • Carbohydrates

    • Elements: CHO (1:2:1 ratio)

    • Monosaccharide

      • Pentose

        • Ribose

      • Hexose

        • Glucose (alpha v. beta)

        • Galactose

        • Fructose

      • Be able to recognize the molecular structure of:

        • Pentose v. hexose

        • Alpha v. Beta Glucose

    • Disaccharide

      • Sucrose (Glucose + Fructose)

      • Lactose (Glucose + Galactose)

      • Maltose (Glucose + Glucose)

      • Be able to recognize the molecular structure of a disaccharide

    • Glycosidic linkage

    • Polysaccharide

      • For the 4 major polysaccharides know:

        • Function

        • Organism

        • Monomer Name

        • Descriptors

      • Starch

        • Amylose

          • 1-4 ⍺-glycosidic linkages

        • Amylopectin

          • 1-4 and 1-6 ⍺-glycosidic linkages

      • Glycogen

        • 1-4 and 1-6 ⍺-glycosidic linkages

      • Cellulose

        • 1-4 β-glycosidic linkages

      • Chitin

    • Glycoprotein

      • Functions

      • ABO blood groups

  • Lipids

    • Elements: CHO (VERY little O compared to C and H)

    • Hydrophobic

    • Nonpolar

    • Fats/Oils

      • Triglycerides

      • Ester linkages

      • Glycerol

      • Fatty Acids

        • Saturated fatty acid

        • Unsaturated fatty acid

        • Monounsaturated

        • Polyunsaturated

        • Cis-unsaturated fatty acid

        • Trans-unsaturated fatty acid

        • Know implications of single v. double bonds in fatty acids

      • Adipose tissue

      • Lipid storage in plants/seeds

      • Functions of fats/oils

      • Be able to recognize the molecular structure of:

        • Fatty acids (all types)

        • Triglyceride

    • Phospholipids

      • Hydrophilic

      • Hydrophobic

      • Amphipathic

      • Phospholipid bilayer

      • Structure:

        • 2 fatty acids

        • Glycerol

        • Phosphate head group

        • Ester linkages

      • Be able to recognize the molecular structure of a phospholipid (and know the parts)

      • Be able to draw and label a phospholipid symbol

    • Steroid

      • Cholesterol

      • Steroid hormones

        • Testosterone

        • Oestrogen (estrogen)

      • Functions of steroids

      • Be able to recognize the molecular structure of steroids

    • Waxes

      • Waterproofing

B1.2 Proteins

Content Statements:

  • B1.2.1—Generalized structure of an amino acid

  • B1.2.2—Condensation reactions forming dipeptides and longer chains of amino acids

  • B1.2.3—Dietary requirements for amino acids

  • B1.2.4—Infinite variety of possible peptide chains

  • B1.2.5—Effect of pH and temperature on protein structure

  • B1.2.6—Chemical diversity in the R-groups of amino acids as a basis for the immense diversity in protein form and function

  • B1.2.7—Impact of primary structure on the conformation of proteins

  • B1.2.8—Pleating and coiling of secondary structure of proteins

  • B1.2.9—Dependence of tertiary structure on hydrogen bonds, ionic bonds, disulfide covalent bonds and hydrophobic interactions

  • B1.2.10—Effect of polar and non-polar amino acids on tertiary structure of proteins

  • B1.2.11—Quaternary structure of non-conjugated and conjugated proteins

  • B1.2.12—Relationship of form and function in globular and fibrous proteins

Vocabulary and Topics:

  • Functions (know 1 example of each)

    • Enzymes

    • Transport

    • Structure

    • Defense

    • Receptors

    • Movement

    • Storage

    • Hormones

  • Amino acid

    • Side chain/R group

    • Amino group (NH2)

    • Carboxyl group (COOH)

    • Alpha carbon (∝)

  • Essential amino acids

  • Nonessential amino acids

  • Implications of vegan/vegetarian diets

  • Dipeptide

  • Peptide bond (be able to identify where a peptide bond is found in a dipeptide/polypeptide diagram)

  • Polypeptide

    • N-terminus

    • C-terminus

    • Examples of polypeptides:

      • Lysozyme

      • Glucagon

      • Myoglobin

      • Alpha-neurotoxins

  • Polypeptide v. protein

  • Protein structure/protein folding

    • For each level of protein structure know:

      • The description of the shape

      • The types of bonds involved and what they are between

    • Primary structure (1°)

      • Polypeptide chain

      • Amino acid sequence

      • Peptide bond

    • Secondary structure (2°)

      • Alpha helices

      • Beta pleated sheets

      • Hydrogen bonding

      • Amino acid backbone

    • Tertiary structure (3°)

      • Hydrophobic interactions

      • Ionic bonding

      • Disulfide bridge

      • Hydrogen bonding

      • Side chains

    • Quaternary structure (4°)

      • Non-covalent bonds and interactions

      • 2+ polypeptides

  • Conjugated protein

    • Examples:

      • Haemoglobin

      • Glycoproteins

  • Non-conjugated protein

    • Example:

      • Insulin

      • Collagen

  • Integral protein

    • Know where hydrophobic and hydrophilic side chains are located in relationship to the phospholipid

  • Globular protein

    • Examples:

      • Insulin

      • Enzymes

  • Fibrous protein

    • Example: Collagen

  • Denaturation

    • Know the causes of denaturation

    • Know the impact of denaturation

  • Be able to draw and label:

    • a single amino acid with the following parts: alpha carbon, amino group, carboxyl group, and side chain

    • a diagram showing the formation of a peptide bond (aka show the formation of a dipeptide), be able to label the peptide bond in the diagram

C1.1 Enzymes and Metabolism

Content Statements:

  • C1.1.1—Enzymes as catalysts

  • C1.1.2—Role of enzymes in metabolism

  • C1.1.3—Anabolic and catabolic reactions

  • C1.1.4—Enzymes as globular proteins with an active site for catalysis

  • C1.1.5—Interactions between substrate and active site to allow induced-fit binding

  • C1.1.6—Role of molecular motion and substrate-active site collisions in enzyme catalysis

  • C1.1.7—Relationships between the structure of the active site, enzyme–substrate specificity and denaturation

  • C1.1.8—Effects of temperature, pH and substrate concentration on the rate of enzyme activity

  • C1.1.9—Measurements in enzyme-catalysed reactions

  • C1.1.10—Effect of enzymes on activation energy

  • C1.1.11—Intracellular and extracellular enzyme-catalysed reactions

  • C1.1.12—Generation of heat energy by the reactions of metabolism

  • C1.1.13—Cyclical and linear pathways in metabolism

  • C1.1.14—Allosteric sites and non-competitive inhibition

  • C1.1.15—Competitive inhibition as a consequence of an inhibitor binding reversibly to an active site

  • C1.1.16—Regulation of metabolic pathways by feedback inhibition

  • C1.1.17—Mechanism-based inhibition as a consequence of chemical changes to the active site caused by the irreversible binding of an inhibitor

Vocabulary and Topics:

  • Metabolism

    • Anabolic

    • Catabolic

    • Condensation

    • Hydrolysis

    • Monomer

    • Polymer

    • Endergonic

    • Exergonic

  • Catalyst

  • Enzyme

  • Know 2-3 named examples of catabolic pathways that require enzymes

  • Know 2-3 named examples of anabolic pathways that require enzymes

  • Active site

  • Substrate(s)

  • Activation energy

  • Transition state

  • Enzyme substrate complex

  • Collision theory (molecular motion)

  • Induced fit

  • Enzyme-substrate specificity

  • Denaturation

  • Optimum pH/temperature

  • Enzyme activity graphs

    • Enzyme concentration

    • Substrate concentration

    • pH

    • Temperature

    • Be able to draw and annotate the graphs (and explain)

  • Enzyme inhibition

    • Competitive inhibition

    • Noncompetitive inhibition

      • Allosteric site

    • Know how to distinguish between them in a graph

  • End-product inhibition

    • Isoleucine synthesis = example

  • Mechanism based inhibition

    • Penicillin/penicillin resistance = example