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Chapters 1 thru 8.

Emphasis is on the material presented in lecture. Know the major points in the text so that you can use that information to answer fill-in-the-blank questions.

1. Know optical isomerism including D and L configuration, asymmetric carbon

Interesting Stuff

Chemical Basics

(chiral center), enantiomers, racemates, diasteroisomers,B writing and recognizing structural formulas, maximum number of optical isomers [2n]. etc., including definitions.

2. Know the Henderson-Hasselbalch Equation. pH = PKa log [A-]/[HA]. Know what the terms mean. Know the conditions for optimum buffering capacity. Be able to solve a straight-forward numerial problem.

3. Know Ionic Strength: I = 1/2 E Ci Zi 2. Be able to solve a stright-forward numerical problem concerning ionic strenghth.

4. Be able to describe the different techniques that are used to isolate and characterize biochemical molecules, such as various type of chromatography, electrophoresis, dialysis and centrifugation. In particular know the terms used in describing electrophoresis and centrifugation including the equations. Electrophoresis: u is electrophoretic mobility. u = v/E = z/f [Note: E is electric field strength and is proportional to voltage; v is velocity.]

Centrifugation: M = sRT/D(1-vp) [Note: D is the diffusion constant and equals RT/f.]

5. Know about the biology of the cell and the various procedures for isolating components of cells. Be able to write a list of steps necessary for the isolation of a protein. (A general scheme was presented in class.)

6. Know the structural formulas and names of the 20 amino acids commonly found in proteins. Know the four groups (classes) of aminoacids based on the nature of their R side chains. Know the names of the eight (ten) essential amino acids.

7. Be able to name and write the structural formulas for simple peptides. Know about the nature of the peptide bond. Be able to solve a sequence problem similar to the one worked out in class.

8. Know the functions of proteins as described in the text. Know the classification of proteins based on solubility and shape and the classification system based on the non-amino component(s) of proteins (as presented in class).







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March 21, 2001

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