1. Chapter 2 Test Review Test: 11/13 INBs due 11/15

2.  See Pg 19 of INB  See lab book  Benedict’s, Biuret, iodine test, nonreducing sugar test  Be able to identify positive and negative results  Be able to predict results from known solutions (ex: glucose) Recognize and understand the different tests for macromolecules (including reagents used and analysis of results)

3.  See pg 12 of INB  Be able to identify where carbon 1 is located  Know –OH group orientation is on carbon 1  Distinguish between forms in pictures describe the ring forms of α-glucose and β-glucose

4.  See pg 12 of INB  What rxn forms bonds  What rxn breaks bonds  order of magnitude for carbohydrates (what is smallest, what is largest) describe the formation and breakage of a glycosidic bond with reference both to polysaccharides and to disaccharides including sucrose

5.  See pg 12 of INB  Amylose: structure and bonds  Amylopectin: structure and bonds  Glycogen: structure, bonds, biological importance  Starch: structure, bonds, biological importance  Cellulose: structure, bonds, biological importance describe the molecular structure of polysaccharides including starch (amylose and amylopectin), glycogen and cellulose and relate these structures to their functions in living organisms

6.  See pg 16 of INB  What are 2 components of triglycerides  How are phospholipids diff. than triglycerides  Know solubility in water (hydrophobic/hydrophilic)  Biological importance of both  What makes a fatty acid unsaturated/saturated and biological significance describe the molecular structure of a triglyceride and a phospholipid and relate these structures to their functions in living organisms distinguish between saturated and unsaturated fatty acids and lipids

7.  See pg 17 of INB  What are the 3 parts of an amino acid  Where and how does a peptide bond form  How does a peptide bond break describe the structure of an amino acid and the formation and breakage of a peptide bond

8.  See pg 17 of INB  Know diffs. Between protein structures  Bonds involved in each structure  Biological importance of specificity in structure  Possible implication of DNA mutations explain the meaning of the terms primary structure, secondary structure, tertiary structure and quaternary structure of proteins and describe the types of bonding (hydrogen, ionic, disulfide and hydrophobic interactions) that hold the molecule in shape

9.  See pg 17 on INB  Importance of iron in the hemoglobin molecule  Structure of hemoglobin (biological significance w/ mutation)  Distinction between collagen molecules and collagen fibers  Biological significance of collagen describe the molecular structure of hemoglobin as an example of a globular protein, and of collagen as an example of a fibrous protein and relate these structures to their functions

10.  See pg 14-15 in INB  SAQ 2.6  Properties of water that lead to biological significance describe and explain the roles of water in living organisms and as an environment for organisms

11.  Practical skills: see pg 3 in INB  Relate knowledge to Ch.1 or word problems  Remember: all PAST knowledge learned is fair game for future exams (this class is cumulative, and you should expect your tests to be as well) use the knowledge gained in this section in new situations or to solve related problems