General Biochemistry I

1. Explain the relationship between amino acids, peptides, and proteins.
2. Describe the structural features and properties of amino acids.
3. Explain the formation and properties of peptide bonds.
4. Describe the different levels of protein structure and the forces that stabilize them.
5. Explain the principles and techniques used for separating and sequencing peptides and proteins.
6. Explain the nature of enzymes and enzyme-catalyzed reactions.

13 weeks, about 43 hours in total. Yours will differ.

1. Week 1Module 1: Amino Acids

   • Unit 1: Amino Acids as Building Blocks of Proteins · 2 hours

     Define amino acids and their role as building blocks of proteins.. Explain the occurrence of amino acids in nature.. Describe the basic structure of amino acids, including the naming of carbon atoms and chirality.. Write the structures of common amino acids like Glycine, Alanine, and Serine..

   • Unit 2: Classification of Amino Acids · 2 hours

     Classify amino acids based on their structures, polarity, and nutritional requirements.. Identify and describe the structures of all common amino acids.. Distinguish between polar and nonpolar amino acids.. Explain the difference between essential and non-essential amino acids..

2. Week 2Module 1: Amino Acids

   • Unit 3: Properties of Amino Acids · 2 hours

     Discuss the physical properties of amino acids, including their response to heat and solubility.. Explain the optical activity of amino acids and their absorption of light.. Describe the acid-base properties of amino acids and their behavior in solution.. Interpret the titration curve of simple amino acids and understand the concept of isoelectric point..

   • Unit 4: Chemical Reactions of Amino Acids · 2 hours

     Describe the reactions of α-carboxyl and α-amino groups in amino acids.. Explain specific reactions for different functional groups in amino acid side chains.. Discuss reactions such as disulfide bond formation, xanthoproteic reactions, and Sakaguchi reaction.. Understand the application of these reactions in identifying and quantifying amino acids..

3. Week 3Module 1: Amino Acids

   • Unit 5: Ph, Pka and Buffering Capacity of Amino Acids · 3 hours

     Define pH and use its mathematical expression to perform calculations.. Explain the dissociation of weak acids and the concept of pKa.. Define buffer solutions and describe how they maintain pH.. Solve problems using the Henderson-Hasselbalch equation.. Understand the role of amino acids as biological buffers..

4. Week 4Module 2: Peptides

   • Unit 1: Peptides-Formation and Nomenclature · 2 hours

     Define peptide and explain how peptides are formed through peptide bonds.. Describe the nature of the peptide bond and its properties.. Explain how peptides are named according to their amino acid residues.. Differentiate between peptides and proteins based on molecular weight..

   • Unit 2: Properties, Examples and Functions Of Biological Peptides · 2 hours

     State the properties of peptides, including their ionic and acid-base characteristics.. List common biologically active peptides and associate them with their specific functions.. Explain the titration curves and isoelectric points of peptides.. Provide examples of biological peptides such as glutathione, oxytocin, and glucagon..

5. Week 5Module 2: Peptides

   • Unit 3: Separation of Peptides I · 3 hours

     State the principles of peptide/protein purification.. Explain how peptides are separated based on solubility using salting out techniques.. Describe peptide purification techniques based on molecular size, including dialysis, ultracentrifugation, and gel filtration.. Understand the preliminary steps to peptide purification, such as cell disruption and centrifugation..

6. Week 6Module 2: Peptides

   • Unit 4: Separation of Peptides II · 3 hours

     Define terms like electrophoretic mobility and isoelectric pH in relation to protein separation.. Differentiate between SDS-polyacrylamide gel electrophoresis and isoelectric focusing.. Describe the procedure of affinity chromatography.. Give examples of various ion exchangers and explain their use in ion exchange chromatography..

7. Week 7Module 2: Peptides

   • Unit 5: Peptide Sequencing · 3 hours

     Outline the general steps for sequencing peptides and proteins.. Describe the preliminary steps to sequencing, including establishing the number of polypeptide chains and cleaving disulfide bridges.. Explain the Edman degradation procedure and its importance in determining amino acid sequences.. Discuss the methods for separating and purifying small peptides for sequencing..

8. Week 8Module 3: Proteins

   • Unit 1: Proteins Nature, Properties, Examples and Biological Functions · 3 hours

     Describe the nature of proteins as polymers of amino acids.. State the basic properties of proteins, including molecular weight, UV absorption, and charge.. Give examples of proteins such as hemoglobin, albumin, and keratin.. Outline the biological functions of different proteins, including transport, structural support, and catalysis..

9. Week 9Module 3: Proteins

   • Unit 2: Structural Levels of Proteins · 3 hours

     Enumerate all the levels of protein structure: primary, secondary, tertiary, and quaternary.. Define the primary structure of a protein as its amino acid sequence.. Describe the different conformations of secondary structure, including α-helix and β-conformation.. Explain the three-dimensional arrangement of atoms in protein tertiary structure.. Discuss the interactions of subunits of polypeptides in quaternary structure..

10. Week 10Module 3: Proteins

    • Unit 3: Stability of Proteins –The Roles of Noncovalent Forces · 3 hours

      Explain the process of protein folding and the role of molecular chaperones.. Enumerate the noncovalent forces that participate in protein stability: hydrophobic interaction, hydrogen bonding, electrostatic forces, and van der Waals forces.. Explain how the compromise of these forces leads to denaturation of proteins' native conformations.. Describe the effects of denaturing agents such as heat, pH changes, detergents, and organic solvents..

11. Week 11Module 3: Proteins

    • Unit 4: Classification of Proteins · 3 hours

      Discuss the criteria for classifying proteins: biological functions, structural complexity, and shape.. List the major functional classes of proteins and give their biological functions: catalytic, transport, structural, regulatory, storage, scaffold, and protective.. Differentiate between simple and conjugated proteins.. Give examples of globular and fibrous proteins..

12. Week 12Module 3: Proteins

    • Unit 5: Enzymes, Co-Enzymes and Vitamins · 3 hours

      Define enzymes and name some examples.. Mention the major classes of enzymes and their functions.. Outline the key properties of enzymes, including their catalytic power, specificity, and sensitivity to temperature and pH.. Explain how enzymes perform their work by lowering activation energy and forming enzyme-substrate complexes.. Differentiate the roles of co-enzymes, co-factors, and vitamins in relation to enzyme activity..

13. Week 13Course Review

    • Final Revision · 4 hours

      Review all modules and units.. Focus on key concepts and definitions.. Complete any outstanding assignments.. Prepare for final examinations..