Introduction to Physiology

LECTURE OUTLINE

I. COURSE OVERVIEW

    A. Textbook
    B. Course description
    C. Prerequsites for the course
    D. Exams, grading, lab, etc.
       1. i>clickers
       2. Facilitation sessions 

II. INTRODUCTION TO PHYSIOLOGY

   A. What is physiology?
      1. Illness results when physiological mechanisms fail
   B. Levels of biological organization
   C. Four themes in physiology
      1. Homeostasis
            a. Homeostasis requires that a control system regulates a parameter
      2. Structure-function relationships exist
            a. Compartmentalization at various levels of biological organization
            b. Division of labor
      3. Communication permits coordination of events and homeostasis
      4. Biological energetics (=metabolism)
            a. Food catabolism provides energy to produce energy-rich ATP
            b. Work and growth then utilize ATP

III. BIOMOLECULES

   A. Carbohydrates
     1. Energy rich compounds important in metabolism
   B. Lipids 
     1. Energy rich compounds important in metabolism
     2. Chemical structure of fats
           a. Saturated and unsaturated fats 
   C. Amino acids, Peptides, and Protein
     1. There are 20 amino acids that polymerize to form proteins
           a. Characteristics of amino acids and proteins
     2. Levels of protein organization
           a. Primary, Secondary, Tertiary, and Quaternary (e.g., globular)
     3. How do proteins function in living systems?
     4. Proteins often work in a "lock and key" fashion (=induced fit model)
           a. Functional characteristics

IV. PROTEIN INTERACTIONS

   A. Some definitions--ligand and binding site
     1. Law of mass action
     2. Binding sites can be saturated
          a. Competitive agonists and competitive antagonists
          b. Cofactors promote ligand binding
   B. Affinity of a ligand for its protein
     1. Two states exist
     2. At equilibrium, the rate of association equals the rate of dissociation
     3. Kd (=Dissociation coefficient; also, Keq)
          a. Significance of Kd--Development of specific drugs
   C. Allosteric (=Noncompetitive) Effects
     1. Alter protein function at a location other than the binding site
   D. Summary of protein characteristics

BASIC FACTS AND TERMS
1. Explain the four themes of physiology that will be covered in this course? Give at least 2 examples of each theme.
2. What are the levels of biological organization studied in Human Physiology? Give an example for each level.

3. What are the chemical characteristics of simple sugars, glycogen, glycerol, fatty acids, fats, amino acids, peptides, polypeptides, and protein? In what ways is each important to normal cell function (List as many as you know)?

4. Define and give the physiological significance (how or why it is important) for the following terms:
• Crossover study
• Placebo
• Blind and Double-blind studies
• Mole
• Homeostasis
• Unsaturated and saturated fats
• Primary structure of a protein
• Secondary structure of a protein
• Tertiary structure of a protein
• Quaternary structure of a protein
• Agonist
• Antagonist
• Polar and nonpolar molecules
• Hydrogen bonds and Van der Walls Forces
• Cofactor
• K_d (=K_eq)


CONCEPTS

5. What is the Law of Mass Action? And how does it apply to a binding site? Explain. Think of at least three physiogical processes where the Law of Mass Action applies?

6. Compare and contrast the functional characteristics of competitive and allosteric binding (= non-competitive) . Give examples of each.

7. What are some of the difficulties associated with research on humans? See pages 10-11 in Silverthorn.

8. Read about pH in the Silverthorn (pages 37-38). What is the normal pH of the blood and extracelluar fluid? Other body fluids?.

   
   REASONING AND PROBLEM SOLVING

9. Why is big pharma so interested in the binding properties of a ligand? How can that information be used in development of new drugs? Explain and give examples to defend your arguments.
10. What evidence indicates that ligand binding is a physical association (i.e., a "lock and key" relationship) with a protein, rather than the formation of a chemical bond? List all lines of evidence.
11. What effect would adding a competitive inhibitor have on the binding curve (Fig. 2-23) for a ligand? Assume that protein concentration is unchanged.

12. You have developed a new drug that you think is more effective than existing drugs. How would you go about proving that this drug is more effective?