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MOLECULES OF LIFE CH 4 AND 5 Carbon is the building block of the molecules of life Chemistry of Carbon I. A. B. Functional Groups Group of atoms linked to carbon that have specific properties Hydroxyl ( OH) o Forms hydrogen bonds Carboxyl (COOH) o Forms ionic bonds Amino (NH2) o Forms ionic bonds Sulfhydryl (SH) o Forms covalent bonds Phosphate (PO4) o Forms covalent bonds o C. Macromolecules Large molecules many of which are polymers Polymer: a macromolecules made of repeating units called monomers Macromolecules are made by dehydration reactions: linking of monomers together with the removal of water Macromolecules are broken down by hydrolysis reactions: breakdown of a macromolecule with the addition of water The 4 macromolecules that make up all living things are: o Proteins o Carbohydrates o Lipids o Nucleic acids II. Carbohydrates A. Monosaccharides 1. structure 2. isomers 3. function B. Disaccharides 1. Structure 2. Function C. Polysaccharides 2 groups of polysaccharides Storage: starch and glycogen Structural: cellulose chitin 1. Storage polysaccharides a. function store glucose for later use b. structure Glycogen Starch 2. structural polysaccharides a. cellulose b. chitin III. Lipids Diverse group of hydrophobic molecules B. Triglycerides (fats and oils) 1. structure 2. Fatty Acid Long chain of C and H with a carboxyl group Usually 14 to 20 Cs Fatty acids can be o Saturated: o Monounsaturated: o Polyunsaturated: 3. C. D. E. Function Phospholipids 1. Structure 2. Property Amphiphathic: 3. Function: Waxes Function as protective barrier Steroids Function as chemical messengers IV. Proteins Large polymer made of repeating monomers called amino acids A. Functions of Proteins Enzymes: catalyze cell’s reactions Defense: antibodies destroy foreign invaders Transport: move molecules around body and into and out of cells Support and structure: long fibrous proteins in hair nails skin Movement: contractile proteins in cells Regulation: proteins involved in maintaining homeostasis B. Amino Acids 1. general structure 2. Groups of amino acids: based on the characteristics of R group Nonpolar Glycine (Gly or G) Alanine (Ala or A) Leucine (Leu or L) Valine (Val or V) Isoleucine (Ile or I) Proline (Pro or P) Methionine (Met or M) Phenylalanine (Phe or F) Trypotphan (Trp or W) Polar Serine (Ser or S) Threonine (Thr or T) Cysteine (Cys or C) Tyrosine (Tyr or Y) Asparagine (Asn or N) Glutamine (Gln or Q) Electrically charged Acidic Aspartic acid (Asp or D) Basic Glutamic acid (Glu or E) Lysine (Lys or K) Arginine (Arg or R) Histidine (His or H) 3. C. Linking of amino acids Linked together by dehydration reactions Protein Structure 1. General rules on protein folding 2. There are 4 levels of protein structure a. primary structure b. secondary structure c. Tertiary structure d. Quaternary structure Special proteins called chaperonins help proteins fold into their secondary and tertiary structures All proteins have primary and secondary structure Most proteins have tertiary structure Some proteins have quaternary structure 3. Protein unfolding V. Nucleic Acids The information molecules Contain and express all of the hereditary info A. Structure Long chains of nucleotides linked via dehydration reactions B. Nucleotides Made of a: 5 carbon sugar Phosphate group One of 4 bases C. Function DNA: RNA: