Course Content - Unit Materials
- Objectives:
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- If given an amino acid, be able to predict its structure under physiological conditions and be able to classify it as either hydrophobic or hydrophilic based on the interactions that its side chain can have with other side chains and with water.
- Be able to join amino acids together with condensation reactions to form a polypeptide.
- Be able to describe the interactions that stabilize to the major forms of secondary structure, the α-helix and the β-sheet.
- Be able to discuss the formation of protein tertiary structure in light of the non-covalent interactions that can take place between a polypeptide's side chains.
- Be able to describe what protein denaturation is and discuss the agents that can lead to protein denaturation.
- Be able to describe how an enzyme can serve as a catalyst and how factors can affect its activity.
- Be able to disuss the nutritional sources of amino acids the distinction between essential and non-essential amino acids.
- Readings
- Chapter 14-1,2,3,4,5,6
- Class Overheads, Fall 2015
- 11.-16. November, 2015
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- PDF to View Online
- PDF to Print
- Homework
- Unit 10 Mastery and Problem Assignment (due 16. Nov., deadline 23. Nov.)
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