Ch. 5 Warm-Up Activity What are the 4 biologically important organic compounds, their building blocks and an example of each? What is the difference between.

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Ch. 5 Warm-Up Activity What are the 4 biologically important organic compounds, their building blocks and an example of each? What is the difference between dehydration synthesis and hydrolysis? When are each used? What are the 4 structural levels of a protein and what bonds are involved in each? What does it mean when a protein has been denatured? What are some possible causes for this to happen?

The Structure and Function of Large Biological Molecules Chapter 5 The Structure and Function of Large Biological Molecules

You Must Know The role of dehydration synthesis in the formation of organic compounds and hydrolysis in the digestion of organic compounds. How to recognize the 4 biologically important organic compounds (carbs, lipids, proteins, nucleic acids) by their structural formulas. The cellular functions of all four organic compounds. The 4 structural levels of proteins How proteins reach their final shape (conformation) and the denaturing impact that heat and pH can have on protein structure

ie. amino acid  peptide  polypeptide  protein Monomers Polymers Macromolecules Small organic Used for building blocks of polymers Connects with condensation reaction (dehydration reaction) Long molecules of monomers With many identical or similar blocks linked by covalent bonds Giant molecules 2 or more polymers bonded together ie. amino acid  peptide  polypeptide  protein larger smaller

(Condensation Reaction) Dehydration Reaction (Condensation Reaction) Hydrolysis Make polymers Breakdown polymers Monomers  Polymers Polymers  Monomers A + B  AB AB  A + B + H2O + + H2O +

Differ in position & orientation of glycosidic linkage I. Carbohydrates Fuel and building material Include simple sugars (fructose) and polymers (starch) Ratio of 1 carbon: 2 hydrogen: 1 oxygen or CH2O monosaccharide  disaccharide  polysaccharide Monosaccharides = monomers (ie. glucose, ribose) Polysaccharides: Storage (plants-starch, animals-glycogen) Structure (plant-cellulose, arthropod-chitin) Differ in position & orientation of glycosidic linkage

The structure and classification of some monosaccharides

Linear and ring forms of glucose

Examples of disaccharide synthesis

Storage polysaccharides of plants (starch) and animals (glycogen)

Structural polysaccharides: cellulose & chitin (exoskeleton)

II. Lipids Fats (triglyceride): store large amounts of energy (2x carbohydrates), cushions organs and insulates body Glycerol + 3 Fatty Acids saturated, unsaturated, polyunsaturated Steroids: cholesterol and hormones Phospholipids: cell membrane hydrophilic head, hydrophobic tails creates bilayer to form cell membrane Hydrophilic head Hydrophobic tail

Ester linkage: between OH & COOH Long HC chain: -Polar or non-polar? -Hydrophilic or hydrophobic?

Have some C=C, result in kinks Saturated Unsaturated Polyunsaturated “saturated” with H Have some C=C, result in kinks In animals In plants Solid at room temp. Liquid at room temp. Eg. butter, lard Eg. corn oil, olive oil

Steroids include cholesterol (shown above) which is the building block for steroid hormones and component of cell membranes

The structure of a phospholipid

Hydrophobic/hydrophilic interactions make a phospholipid bilayer

Overview of protein functions

Overview of protein functions

Proteins: polymers made of amino acid monomers

III. Proteins Four Levels of Protein Structure: Primary Amino acid (AA) sequence 20 different AA’s peptide bonds link AA’s

Four Levels of Protein Structure (continued) Secondary Gains 3-D shape (folds, coils) by H-bonding Alpha (α) helix, Beta (β) pleated sheet

Four Levels of Protein Structure (continued) Tertiary Bonding between side chains (R groups) of amino acids H & ionic bonds, disulfide bridges, van der Waals interactions

Four Levels of Protein Structure (continued) Quaternary 2+ polypeptides bond together

amino acids  polypeptides  protein Bonding (ionic & H) can create asymmetrical attractions

Chaperonins assist in proper folding of proteins

Protein structure and function are sensitive to chemical and physical conditions Unfolds or denatures if pH and temperature are not optimal

change in structure = change in function

Function: carry hereditary info IV. Nucleic Acids Function: carry hereditary info DNA RNA Double stranded helix N-bases: A, G, C, Thymine Stores hereditary info Longer/larger Sugar: deoxyribose Single stranded N-bases: A, G, C, Uracil Carry info from DNA to ribosomes tRNA, rRNA, mRNA, RNAi Sugar: ribose

Nucleotides: monomer of DNA/RNA 3 parts: -nitrogen base -pentose sugar -ribose -deoxyribose -P04 group

Nucleotide phosphate A – T Nitrogenous base G – C 5-C sugar Purines Pyrimidines Adenine Guanine Cytosine Thymine (DNA) Uracil (RNA) Double ring Single ring 5-C sugar

Building the polymer

Nucleic polymer Backbone Sugar to PO4 bond Phosphodiester bond new base added to sugar of previous base Polymer grow in one direction N bases hang off the sugar-phosphate backbone

Pairing of nucleotides Nucleotides bond between DNA strands H bonds Purine :: Pyrimidine A :: T 2 H bonds G :: C 3 H bonds

DNA  RNA  protein: a diagrammatic overview of information flow in a cell.