General Biochemistry A

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.






General characterization

Code

10650

Credits

6.0

Responsible teacher

Pedro António de Brito Tavares

Hours

Weekly - 4

Total - 56

Teaching language

Português

Prerequisites

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

Bibliography

Main references

LEHNINGER PRINCIPLES OF BIOCHEMISTRY
Nelson, D.L., & Cox, M.M.
W.H. Freeman and Company, San Francisco, 7th ed., 2017

FUNDAMENTALS OF BIOCHEMISTRY. LIFE AT THE MOLECULAR LEVEL
Voet, D., Voet, J.G. & Pratt, C.W.
John Wiley & Sons, Inc., New York, 5th ed., 2016

BIOCHEMISTRY
Berg, J.M., Tymoczko, J.L., & Stryer L.
W. H. Freeman and Company, San Francisco. 8th ed., 2015

BIOCHEMISTRY. A SHORT COURSE
Berg, J.M., Tymoczko, J.L., & Stryer L.
W. H. Freeman and Company, San Francisco. 3rd ed, 2015

 

Teaching method

The course is organized in lectures, laboratory classes and workshops. The students must apply the concepts developed in the lectures to the analysis of the experimental results obtained in the laboratory and to problem solving in the workshops.

Evaluation method

The final grade is calculated according to the following formula:

                           Final Grade = 0.80 x Theoretical Grade + 0.20 Practical Grade

Students will pass the course unit with a grade greater than or equal to 9.5 values.

Attendance(frequency):

1. Mandatory attendance of the 5 practical laboratory sessions

  • The student''''s punctuality, the preparation of laboratory classes, and the execution of the experimental work, will contribute to obtaining the frequency

2. Attendance of 70% of theoretical classes and 70% of theoretical-practical classes (only for 1st enrollment students)

Theoretical grade:

1. Continuous assessment by 3 tests

2. Assessment by final exam

  • To pass the subject, the theoretical grade must be greater than or equal to 8.0.

Practical grade:

3 mini-tests at the end of each theoretical test

  • No minimum grade is required for the practical component.

Important notes:

  • The scores for all assessment elements will be rounded to the nearest tenth; the grades of each component will enter the final classification formula also rounded to the nearest tenth.
  • Students who have not passed the continuous assessment are admitted to the final exam. In the exam, only the T component is evaluated. To be successful, the classification in this exam must be equal to or greater than 8.0.
  • Improvement of the final grade is performed on the final exam and only on the T component.


In any case, the UC regent reserves the right to carry out an oral exam, for final approval, to any student enrolled in the course.

Subject matter

4.  Summary of the lectures:

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.
12 – Photosynthesis.

Problem-solving sessions:
1 -Amino acid and Proteins – Acid-base properties
2 - Structure polypeptides and proteins.
3 - Enzyme kinetics
4 - Nucleic acids. Biological membranes.
5 – Metabolism

Laboratory sessions :

1 – Amino acid titrations
2 – Separation of biological compounds by chromatography
    A – Gel filtration
    B – Ionic Chromatography
3 – Enzymatic characterization of Fusarium graminearum beta-glucosidas

4 - Protein determination

Programs

Programs where the course is taught: