Term 1

A1.1.1—Water as the medium for life 

A1.1.2—Hydrogen bonds as a consequence of the polar covalent bonds within water molecules

A1.1.3—Cohesion of water molecules due to hydrogen bonding and consequences for organisms

A1.1.4—Adhesion of water to materials that are polar or charged and impacts for organisms

A1.1.5—Solvent properties of water linked to its role as a medium for metabolism and for transport in plants and animals

A1.1.6—Physical properties of water and the consequences for animals in aquatic habitats

1.1.7—Extraplanetary origin of water on Earth and reasons for its retention

A1.1.8—Relationship between the search for extraterrestrial life and the presence of water

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

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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 

A1.2.1—DNA as the genetic material of all living organisms

A1.2.2—Components of a nucleotide

A1.2.3—Sugar–phosphate bonding and the sugar–phosphate “backbone” of DNA and RNA

A1.2.4—Bases in each nucleic acid that form the basis of a code

A1.2.5—RNA as a polymer formed by condensation of nucleotide monomers

A1.2.6—DNA as a double helix made of two antiparallel strands of nucleotides with two strands linked by hydrogen bonding between complementary base pairs 

A1.2.7—Differences between DNA and RNA

A1.2.8—Role of complementary base pairing in allowing genetic information to be replicated and expressed

A1.2.9—Diversity of possible DNA base sequences and the limitless capacity of DNA for storing information

A1.2.10—Conservation of the genetic code across all life forms as evidence of universal common ancestry 

A1.2.11—Directionality of RNA and DNA

A1.2.12—Purine-to-pyrimidine bonding as a component of DNA helix stability

A1.2.13—Structure of a nucleosome

A1.2.14—Evidence from the Hershey–Chase experiment for DNA as the genetic material

A1.2.15—Chargaff’s data on the relative amounts of pyrimidine and purine bases across diverse life forms