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General Biochemistry B

Objectives

Aims:

After the course it is expected that the students know the basic structural features of the major biological macromolecules and understand the physical-chemical principles underlying the relationship between structure and function. The students should also understand the strategy, regulation, and bioenergetics of the central metabolic pathway. It is expected that the students apply the concepts developed in the lectures to the analysis of experimental results obtained in the laboratory classes and to problem solving.

At the end of this course the student should:

  • understand the structural organization and composition of proteins;
  • know the techniques used in the purification and characterization of proteins and how to evaluate the efficiency of a purification process;
  • understanding the mechanisms of oxygen transport/storage by hemoglobin and myoglobin and distinguish between cooperative and uncooperative interaction;
  • using mathematical models, to calculate the kinetic parameters of Michaelis-Menten enzymes in the absence and presence of inhibitors, and evaluate the effect of temperature and pH on the reaction rate;
  • know the structures of simple sugars and polysaccharides;
  • Understand the structure of nucleic acids and their physicochemical properties; the flow of genetic information from gene to protein;
  • be aware of the structures of lipids and their organization; biological membranes and biological transport;
  • Understand metabolism and bioenergetics: central metabolic pathway and ATP synthesis (glycolysis and gluconeogenesis, the citric acid cycle, electron transport chain and ATPS synthesis)

General characterization

Code

7321

Credits

6.0

Responsible teacher

José Luís Capelo Martinez

Hours

Weekly - 4

Total - 55

Teaching language

Português

Prerequisites

Strongly recommended a basic background of organic chemistry and general chemistry.

Bibliography

PRINCIPLES OF BIOCHEMISTRY
Voet, D., Voet, J.G. & Pratt, C.W.
John Wiley & Sons, Inc., New York, 3rd ed. 2008

BIOCHEMISTRY
Lubert Stryer
W. H. Freeman and Company, San Francisco. 6th Ed. 2007

 

LEHNINGER PRINCIPLES OF BIOCHEMISTRY
Nelson, D.L., & Cox, M.M.
W.H. Freeman and Company, San Francisco, 5th ed. 2008

Teaching method

Lectures (02:00, 14 weeks) and theoretical-practical lessons (03:00, 4 weeks), with the help of slides in Powerpoint; the talks are part of the teaching programme and the discussion and resolution of problems and questions are about matters of discipline. Laboratory sessions and seminars (03:00, 5 weeks) in groups of 3 to 4 students.

The concepts developed in the lectures are applies to the analysis of the experimental results obtained in the laboratory and to problem solving in the TP classes. The preparation of the working sessions andlaboratory classes is an important part of the work inautonomy by the student, but is subject to review and correction by the teacher.

Evaluation method

Evaluation

The final evaluation is the result of a theoretical examination paper (75%) ,a practical component (20%) that accounts for the laboratory work and a 10% accountig for participation.. The attendance to the laboratory classes is compulsory besides 70% of lectures (T and TP).

Subject matter

Syllabus

  1. Introduction to Biochemistry (Biological structures, metabolic pathways, expression and transmission of genetic information). 
  2. The amino acids properties: peptide bonds - Classification and characteristics. Acid-base properties
  3. Levels of protein structure organization: primary, secondary (alpha helices, beta sheets and other structural elements), tertiary and quaternary structures. Protein isolation, purification and sequencing.
  4. Fibrous proteins (Keratin, silk, collagen) and globular protein (Myoglobin and hemoglobin) 
  5. Structure-function mechanisms in the hemoglobin. 
  6. Enzyme kinetics Inhibition and regulation.
  7. Enzyme mechanisms: Lisozima, Ribonuclease, Carboxipeptidase, Quimotripsina. 
  8. Carbohydrates (Classification and function). Monosaccharides and structural and storage polysaccharides (cellulose, chitin, starch and glycogen). Glycoproteins (Proteoglycans and glycosylated proteins). 
  9. Biological Membranes: structure and dynamic. Biological transport: Passive-mediated transport, active-transport. Ion channels, Uniport, symport, and antiporte systems. 
  10. Nucleic acids (RNA and DNA): structure and function. Denaturation and Renaturation of nucleic acid. Restriction endonucleases: the chain- terminator method of DNA sequencing and Manual sequencing. Recombinant DNA technology. PCR and site-directed mutagenesis techniques. 
  11. Metabolism (Catabolism and anabolism) and Bioenergetics: Glycolysis, lactic and alcoholic fermentation, Citric acid Cycle, electron transport chain and oxidative phosphorylation.

Problem-solving sessions

  1. Amino acid and proteins – Acid-base properties 
  2. Enzyme kinetics
  3. Nucleic acids. Liids and biological membranes. Biological transport.
  4. Metabolism and bioenergetics

Laboratory sessions

4 laboratory sessions:

  1. Amino acid titrations 
  2. Separation of biological compounds by chromatography
  3. Carbohydrate identification
  4. Enzymatic characterization of Fusarium graminearum beta-glucosidase