Review the "basics" on proteins as you develop an awareness of basic structure of amino acids and proteins. You will consider the classification and digestion and metabolism of important proteins. You will learn about protein electrophoresis and immunoelectrophoresis, as well as other protein methods, expected values, and clinical significance.
PEP hours: 16
CPS/ART credits: 0
Course Type: Express
Start Date: Upon registration
Completion: Up to 52 weeks
Delivery: PDF via email
Equipment: Computer with Internet is required
- Describe the structure of amino acids and their relationship to the structure of protein.
- Recognize an amino acid by its basic structure and know the names of the standard amino acids.
- Illustrate the following properties of amino acids: ionization, acid-base chemistry, and peptide bond formation.
- Describe the different ways to classify proteins.
- Describe protein structure in terms of primary, secondary, tertiary and quaternary structures.
- Describe the different aspects of protein denaturation, precipitation, and degradation.
- Describe the events involved in the digestion of proteins.
- Explain aspects of amino acid metabolism including sites of metabolism, deamination and transamination reactions, and how protein metabolism fits into the overall metabolism picture.
- Explain the principle of the biuret method used for protein quantitation and name other methods used to measure protein.
- Describe the principle of gel and capillary protein electrophoresis.
- Recognize a normal electrophoretic pattern identifying the separated fractions and identify abnormal electrophoretic patterns.
- Explain the clinical utility of protein electrophoresis.
- List the proteins and their function in each electrophoretic fraction and identify abnormal electrophoresis patterns.
- Describe the structure and function of immunoglobulins.
- Describe the principle and procedure of immunofixation.
Author/Instructor: Wendy Mellen, MLT, BSc
Version Date: October 2011