Study-Unit Description

Study-Unit Description



CODE CHE1510

 
TITLE Fundamentals and Applications of Biological Chemistry 2

 
UM LEVEL 01 - Year 1 in Modular Undergraduate Course

 
MQF LEVEL 5

 
ECTS CREDITS 4

 
DEPARTMENT Chemistry

 
DESCRIPTION 1. Nucleosides, Nucleotides and Nucleic acids
    1.1 Nucleoside and nucleotide structure: purine and pyrimidine bases, the phosphodiester and N-glycosidic
          bonds.
    1.2 DNA and RNA structure: deoxyribonucleotides, the DNA double helix, the role of hydrogen bonding and
          electrostatic interactions in complementary base pairing and the higher structure of nucleic acids
    1.3 Nucleotide and nucleic acid biosynthesis
    1.4 Nucleic acid sequencing: the dideoxynucleotide and Maxam/Gilbert methods

2. Amino acids and proteins
    2.1 Structure of amino acids and proteins: different classes of amino acid side groups, 1°, 2°, 3° and 4° structure.
    2.2 Amino acid and protein biosynthesis, catabolism and turnover
    2.3 The role of covalent bonding and noncovalent interactions in protein structure; the amide bond; electrostatic
          forces, hydrogen bonding, Van der Waals forces, hydrophobic forces
    2.4 Proteins and pH: point of zero charge, side group effects, effect of pH on protein charge and solubility,
          applications in electrophoresis and IEF
    2.5 Proteins in solution: the Florey-Huggins theory, thermodynamics of the hydrophobic effect
    2.6 Protein stability: Chemical stability (deamidation, racemisation, proteolysis, oxidation, beta-elimination,
          disulfide exchange), physical stability (denaturation, aggregation, precipitation, adsorption)
    2.7 Case study of proteins I - Enzymes:
          2.7.1 Thermodynamics and kinetics of enzyme reactions: the Michaelis-Menton equation, Lineweaver Burke,
                   Dixon and Eadie-Hofstee plots; kinetics of competitive and noncompetitive inhibition
          2.7.2 Regulatory strategies in enzymes: allosterism, cooperativity, and hysteresis
          2.7.3 Mechanisms of enzyme reactions: ordered vs random, sequential vs ping-pong
    2.8 Case study of proteins II – Monoclonal antibodies
          2.8.1 Gross and fine structure of antibody molecules; heavy chains and light chains, constant and variable
                   regions, hypervariable regions
          2.8.2 Chemistry of antigen-antibody binding: affinity vs avidity, calculation of Ka by Scatchard analysis and
                   nonlinear regression; the immunological importance of Ka
          2.8.3 Monoclonal antibodies and liposome targeting: coupling reactions of liposomes with antibodies,
                   carboxy/amino, hydroxyl/amino, amino/amino, esterification, anhydride formation, sulfhydryl reactions

Reading List

  -  MANN et al. (1994) Natural Products: Their Chemistry and Biological Significance. Pearson Education Ltd. Essex.

 
STUDY-UNIT TYPE Lecture

 
METHOD OF ASSESSMENT
Assessment Component/s Sept. Asst Session Weighting
Progress Test No 15%
Examination (2 Hours) Yes 85%

 
LECTURER/S Claude A. Farrugia

 

 
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