Unit 1: Chemistry of Life 1.1 Water and Hydrogen Bonds Water is polar, meaning it has a partially positive area and a partially negative area. Polar molecules can hydrogen bond with other polar molecules, when the partial + of one attracts the partial – of the other molecule. o Cohesion – water’s attraction to other water molecules o Adhesion – water’s attraction to other polar substances o Surface tension – The relative difficulty in breaking through water’s surface due to hydrogen bonds between water molecules Non-polar molecules have no partial charges, and clump together because they are hydrophobic (waterfearing) 1.3 Introduction to Biomolecules Hydrolysis o The breaking of covalent bonds that join together polymers (big small) o Requires the breaking (lysis) of a water molecule to stabilize the products Dehydration synthesis o The formation of covalent bonds between monomers (building of a polymer) (small large) o Results in the formation of a water molecule as a byproduct. 1.4 Properties of Biomolecules Carbohydrates Lipids Proteins Nucleic Acids Fatty Acids Monomer Monosaccharides Amino Acids Nucleotides Names Glycerol Polymer Polysaccharides Lipids Proteins, Polypeptides Nucleic Acids Names C, H, O C, H, O, N Primary C,H,O (in 1:2:1 ratio) C, H, O, N, P Elements (Phospholipids have P) (Some have S) Long hydrocarbon (usually) Ring-like structure chains Saturated – no C-C double bonds Unsaturated – Contain double bonds, which give the molecule fluidity Structure Examples Sugars, starch, glycogen, cellulose Fats, Oils, Butter Polarity Polar - due to the presence of OH groups Nonpolar - due to the long hydrocarbon chains A central C bonded to: H atom NH2 (Amino) COOH (Carboxyl) R group (Functional) Hemoglobin, Catalase, Lipase Polar or Nonpolar depending on the R group (see back) Nucleotide contains: -sugar -phosphate group -nitrogen base DNA, RNA Polar - due to the sugar, negatively charged phosphate Types of amino acids (based on R-group) o Nonpolar – R group contains mainly C-H bonds o Polar – contains O-H, N-H, or S-H bonds o Basic – positively charged o Acidic – negatively charged 1.5 Structure and Function of Biomolecules (protein structure) The structure of a molecule determines its function. Changing the structure of a molecule can change its function Proteins have 4 structural levels: o Primary (1°) The sequence of amino acids Held together by strong covalent bonds Can only change due to mutations in the DNA or RNA code o Secondary (2°) alpha helices or beta-pleated sheets held together by weak hydrogen bonds (between the amine and carboxyl groups o Tertiary (3°) Folding of the protein caused by interactions between R-groups of the amino acids Strong disulfide bridges form between cysteine amino acids Slightly weaker hydrophobic interactions between nonpolar (hydrophobic) amino acids hiding from polar and/or charged (hydrophilic) amino acids Weaker ionic bonds between basic and acidic amino acids Weak hydrogen bonds between polar amino acids Weak ionic and hydrogen bonds can be affected by high temperatures and changes in pH o Quaternary (4°) When 2 proteins (polypeptides) come together to form a multi-protein complex Held together by weak bonds (similar to tertiary level bonding) that can be affected by temperature and pH 1.6 Nucleic Acids Monomers contain 3 components: o Sugar (Deoxyribose or Ribose) o Phosphate group (always the same) o Nitrogen base (4 different types) DNA is double-stranded and antiparallel and is defined by the 3’ and 5’ end designations (shown below) Double-stranded DNA is held together by hydrogen bonds between complementary bases (C and G) (A and T) Have an overall negative charge due to the negative phosphate group Differences between DNA and RNA o DNA has deoxyribose sugar, RNA has ribose sugar o RNA has base Uracil (U) and DNA has base Thymine (T) o DNA is usually double-stranded, RNA is usually single-stranded pH pH lower than 7 is acidic – Acids have high concentrations of H+ (protons) pH higher than 7 is basic – Bases have low concentrations of H+ (protons)