1. Midterm Review Fall 2007

2. Identify the following monomers:

3. Amino Acids and Proteins What are the main components of an amino acid? Amino Acids are monomers that make up ______________ How do amino acids determine the shape of a protein? How does the shape of a protein determine its function?

4. Two Amino Acids join to form a peptide bond—a chain of amino acids makes up a peptide or protein

5. The Main Components of Amino Acids Contain nitrogen, hydrogen, carbon and oxygen & sometimes Sulpher (CHON or CHONS) Amino group: NH2 Carboxyl group: COOH R Group (variable)

6. There are 20 different amino acids— each with a different R group

7. The specific amino acids determine the shape of the Protein or Peptides

8. 4 levels of protein structure Primary Secondary Tertiary Quaternary

9. Primary Structure The unique sequence of amino acids attached by peptide linkages What could happen if one amino acid is missing or in a different position?

10. Secondary Develops when the protein chain takes a particular shape immediately after formation at the ribosome Parts of the chain become folded and/or twisted The most common shapes: Coiling  alpha helix (ά) Folding  beta helix (β) These shapes are permanent and held in place by hydrogen bonds

11. Tertiary Structure Precise, compact structure, unique to that protein, which arises when the molecule is further folded Types of bonds Hydrogen: hydrogen shared by 2 atoms (weak) Van der Waals: two or more atoms are very close Disulphide: strong covalent bond (SH groups) Ionic: oppositely charged ions

12. Quaternary Structure When two or more proteins become held together, forming a complex, biologically active molecule Example hemoglobin, consisting of 4 polypeptide chains held around a non- protein group

13. Levels of Protein Structure

14. What is an enzyme An Enzyme IS a Protein It is a biological catalyst

15. Why is shape important to proteins, specifically Enzymes? Due to its precise shape and distinctive chemical properties, each enzyme is specific for a certain substrate or a VERY small group of substrate molecules.

16. Shape can be used positively and negatively Positive If a protein’s active site and a substrate match, they will bond and react Negative If a protein’s active site and an “imposterer” match the intended reaction will not occur If another site on the protein is filled, the intended reaction will not occur

17. Illustrate each type of inhibition— Why is protein shape important? Competitive Inhibition Non-Competitive Inhibition Allosteric Inhibition End-Product inhibition (negative feedback)

18. How can a protein lose its shape? Denaturation is a structural change in a protein that alters its 3-D shape and causes the loss of its biological properties

19. Cell Theory 1. All organisms are composed of cells (this does not mean that we have some cells--it means that we are made of cells) 2. All cells come from pre-existing cells (there is no such thing as a cell that comes from something other than a cell) 3. Cells are the basic unit of structure and function (cells are the smallest unit of life that fulfill all the requirements of life)

20. Two major types of cells Prokaryotes Simple Small No nucleus No membrane-bound organelles Bacteria (archea and eubacteria Reproduce by binary fission All unicellular NOT VIRUSES Eukaryotes More complex Larger Nucleus Membrane-bound organelles Plants,Animals, & Fungi,Protists Reproduce by mitosis Unicellular or multicellular