List a Carbohydrate Monomer List a Carbohydrate Polymer List a Lipid Monomer List a Lipid Polymer

Organic Compound Quiz

11. Hydrogen bonds can form between regions of polar molecules that are a. nonpolar. b. negatively charged. c. oppositely charged. d. uncharged (neutral). 12. An ion is formed when an atom gains or loses a. protons. b. neutrons. c. bonds. d. electrons.

2.3 Carbon Based Molecules Chemistry of Life 2.3 Carbon Based Molecules

Properties of Carbon Carbon forms covalent bonds with up to four other atoms, including other carbon atoms.

Monomer – Small molecule that is a single unit in a much larger molecule. Polymer –Large molecule (macromolecule) formed from many monomers bonded together.

Is it a Monomer or Polymer?

Carbohydrate Type of Molecule Functions Monomers / Polymers Broken down to provide a source of energy Make up plant cell walls Carbohydrate Monomer – Glucose Polymer – Starch – Cellulose

Glucose

Lipid Type of Molecule Functions Monomers / Polymers – Triglyceride Broken down to provide a source of energy Make up cell membranes – Triglyceride – Phospholipid Glycerol + Fatty Acid Lipid

Proteins Type of Molecule Functions Monomers / Polymers Enzymes Transport oxygen muscle movement Proteins

GENERAL CHARACTERISTICS AND IMPORTANCES: • Polymers of amino acids • Each has unique 3-D shape • Vary in sequence of amino acids • Major component of cell parts • Provide support • Storage of amino acids • Receptor proteins; contractile proteins; antibodies; enzymes

BUILDING BLOCKS: Amino acids 20 different amino acids

PEPTIDE BONDS:

PROTEIN CONFORMATION: Unique 3-D shape PRIMARY: Sequence of amino acids Determined by genes (sequence of bases in DNA) SECONDARY: Regular repeated folding of peptide chain Folding stabilized by hydrogen bonds b pleated sheet a helix TERTIARY: Globular proteins Irregular contortion Shape stabilized by H bonds, ionic bonds, hydrophobic interactions, disulfide bridges Enzymes QUATERNARY: Interaction of several Polypeptides Hemoglobin Collagen

Protein Lab Construct a protein with the following Amino Acid sequence. 1 green 4 white 6 yellow 4 white 1 green Primary structure

Protein Lab Now fold the protein so that the polar regions interact with polar regions and nonpolar with nonpolar. Secondary structure

Protein Lab Now bond the two green amino acids together. Tertiary structure

DENATURATION: Changing protein’s shape Change shape = change in activity How? 1. High temperature 2. Chemical agent (acid or base) change in pH 3. Organic solvent

DNA & RNA Store Genetic Information Build Proteins Type of Molecule Functions Monomers / Polymers Nucleic Acids Store Genetic Information Build Proteins DNA & RNA Monomer – Nucleotide Polymer – DNA and RNA

Fatty acids and Glycerol CFA Quiz Standard 1.h Organic Compound List the monomer List a polymer #1 #2 Protein (Ex. Hemoglobin) Nucleic Acid #3 #4 #5 Fatty acids and Glycerol #6 #7 #8 Glycogen, Starch

What elements do Carbohydrates have? What is a main function of Proteins?

Fatty acids and Glycerol CFA Quiz Standard 1.h Organic Compound List the monomer List a polymer #1 PROTEIN #2 AMINO ACID Protein (Ex. Hemoglobin) Nucleic Acid #3 NUCLEOTIDE #4 DNA / RNA #5 LIPID Fatty acids and Glycerol #6 TRIGLYCERIDE PHOSPHOLIPID #7 CARBOHYDRATE #8 GLUCOSE / STARCH Glycogen, Starch

What elements do Carbohydrates have? C H O What is a main function of Proteins? ENZYME / TRANSPORT OXYGEN /MUSCLE

Enzymes

ENZYME PROPERTIES & STRUCTURE Globular proteins Catalysts - speed up chemical rxns by lowering activation energy (energy needed to start rxn) Not used up in chemical rxn Active site = groove or pocket where substrate binds Specific Shape related to function – change shape (denature) enzyme no longer functions Yellow = active site Pink = enzyme

ENZYME ACTION – INDUCED FIT MODEL Enzyme = pink Active site = Yellow Substrate = red Substrate binds to enzyme at active site Enzyme (active site) changes Shape Bonds form between substrate (or break) Product (green) Released Enzyme unchanged & ready to be used again

CFA Quiz 1.h 1) What are enzymes made out of? 2) How do enzymes speed up chemical reactions? 3) What is the optimal temperature for the enzyme represented in the graph? 4) What affect can too high of temperature have on an enzyme?