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Spring 2008 Lecture Schedule
Date Topics   Ch.*
Jan 14 Introduction/Microscopy 1
16 Spectrophotometry 2
21 MLK Day -- No Class  
  23 Fluorescence/Flow Cytometry 3
28 Radiochemistry 4
  30 pH and Buffers 5
4 Luni Gras -- No Class  
6 Centrifugation 6
8 Review Session TBA (Friday)?  
11 Exam I (over 1/14-2/6 material)  
  13 Protein Structure
Differential Solubility
  18 Chromatography 9
20 Membrane Proteins/Detergents 10
25 Electrophoresis/SDS-PAGE 11
27 Electrophoresis/IEF 11
Mar  3 Overview Protein Purification 12
5 Immunization/Adjuvants 13
  10 Immunoprecipitation/Immunoblotting 15
12 Immunofluorescence + others 15
  17   No Class -- Spring Break  
  19   No Class -- Spring Break  
  24 Monoclonal Antibodies 14
28 Exam II (over 2/13-3/24 material)  
  31 Isolation & Analysis of Nucleic Acids 16
2 Restriction Enzymes
  7 Blotting Techniques 19
  9 Polymerase Chain Reaction 20
  14 Recombinant DNA 21
16 Expression of Recombinant Proteins 22
21 DNA Sequencing 23
23 Bioinfomatics 24
28 Proteomics 24
  Exam III (covering 3/31-4/28 material)  

*Refers to chapter numbers in Lecture Notes.


This course provides students with a broad overview to the basic biochemical, molecular and immunological techniques that are commonly used in modern biomedical research. Lectures will describe the theories and principals behind each of the methods in addition to discussing the practical aspects and limitations in executing the various procedures. One of the course objectives is to assist students with their own research by providing them with sufficient background information so that they are able to design experiments and know which methods are best suited for a particular research question or problem. A second course objective is to provide students a better access to the scientific literature in that understanding the methods will allow the students to critically evaluate the results and conclusions of scientific papers. Students anticipating careers involving biological or medical research at any level will benefit from this course.

The course consists of three sections: 1) general biochemical and biophysical methods, 2) analysis and isolation of proteins and immunological procedures, and 3) analysis of nucleic acids and recombinant DNA. The first section will cover some basic biochemical procedures and equipment. Understanding these basic biochemical principals will assist in the discussions on proteins and nucleic acids. The section on characterization of proteins will describe some basic methods used to analyze proteins and provide an overview on protein purification. How to make antibodies and their use in various assays will also be covered. The final section on nucleic acids will describe the basic procedures used in molecular biology with a focus on cloning genes.


There is no required textbook for the course. Lecture notes corresponding to the material covered in class as well as supplemental material are available. Two versions are available on-line in pdf format: 1) a version for printing on one side of the paper and binding on the left (notes.pdf), and 2) a version for printing on both sides of the paper and binding on the left (notes_2p.pdf). The files are large (>200 pages and 2.5 Mb). It is also possible to arrange for printing and binding through Fedex Kinko’s (https://docstore.kinkos.com/tulane_student).


Examinations will be given after each of the three sections. Exam I will worth 80 points and Exams II and III will be worth 100 points each. The format of the examinations will be essay questions and problems. An additional 80 points will be derived from the best eight out of eleven homework assignments.


The class meets from 1:30-2:45 on Mondays and Wednesdays in room 12__ of the Tidewater Building (see #4 on map). See Tropical Medicine Schedule for room scheduling updates.


Mark F. Wiser, Ph.D.
Office: 2224 Tidewater Building (in Suite 2210)
Telephone: 988-2507
email: wiser@tulane.edu

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