Goals

1. To acquire the basic principles of protein biochemistry : how the physico-chemical properties of amino acids and peptides determine the structure and function of proteins. 2. To understand the principles of enzymatic activity and kinetics for simple reactions, and the regulation modes. 3. To acquire the basic principles of carbohydrates biochemistry. 4. To know the following metabolic pathways : glycolysis, glycogenolysis, glycogen synthesis, Krebs cycle and oxydative phosphorylation.

Content

The biochemistry course introduces the basic concepts of biochemistry and particularly the relationship between protein structure and function, highlighting the mechanisms explaining the particular properties of enzymes, i.e. the catalytic activity combined with a high specificity. The basics of enzymatic activity and kinetics of simple reactions (one substrate) are studied, as well as the various regulation modes of enzymatic activity. A part of the course is dedicated to mono- and poly-saccharides and their eventual conjugation to proteins. Metabolic pathways directly linked to glucose catabolism are presented : glycolysis, glycogenolysis, glycogen synthesis, Krebs cycle and oxidative phosphorylations. The importance of enzymatic regulation in a metabolic context is stressed.

Table of contents

1st part : proteins

1. Introduction

2. Amino acids

- Structure and classification

- Optical properties

- Acid-base properties

- Amino acids and proteins separation:

- ion exchange chromatography

- reverse phase chromatography

- chromatographie d’exclusion

- (affinity chromatography) 

- electrophoresis (SDS-PAGE, IEF, Western Blot)

3. Peptides

- Sructure : the peptide bond

- Peptide synthesis (Merrifield)

- Protein sequencing (Edman *, mass spectrometry)

4. Protein structure

- Primary structure

- Secondary structures : a helix, b sheet, b turn

- Tertiary structure

- Fibrillary proteins (ex:  collagen)

- Globular proteins (ex : myoglobin)

- Protein denaturation and renaturation

- Quaternary structure (ex : hemoglobin)

- Physical properties of proteins (solubility, optical properties) 

5. Enzymatic activity

- Catalytic power

- Specificity

- Catalytic mechanism(acid-base, covalent, metal-dependent)

6. Kinetics

- one-substrate reactions

-  Michaelis-Mentem equation and curve

- Lineweaver-Burke transformation

- Enzymatic inhibition

- two-substrate reactions

7. Regulation

- Enzyme abundance (transcriptional, translational controls, enzyme stability) 

- Post-translational modifications 

- Allostéric regulation

- Proteolytic processing of zymogens 

 

2nd part : saccharides

1. Monosaccharides

2. Disaccharides

3. Polysaccharides

- Reserve

- Structure

4. Glycoconjugates

- Proteoglycans

- Glycoproteins

- Glycolipides

 

3rd part : metabolism

1. Metabolism overview

- Introduction

- High energy groups transfer

- Electron transfert

2. Glycolysis

3. Glycogen metabolism

- Glycogenolyis

- Glycogen synthesis

4. Krebs cycle (and the glyoxylate cycle)

 

5. Oxydative phosphorylations

Assessment method

This course introduces the basic concepts of protein biochemistry, and particularly the relationship between structure and function. A large part of the course is dedicated to understand the forces involved in the protein folding and the chemical mechanisms underlying the catalytic mechanism of enzymes. If some knowledge is required, the student will be mainly evaluated at the level of basic concepts and his/her ability to use these concepts to explain the biochemical process. Consequently, the basic principles are very important, but the student must also be able to justify his/her answers during the oral exam, where the question "why ?" will be often asked.

The global note is composed of 16 points for the examination on theory and 4 points for the practical courses.

The practical course evaluation includes : 

- the notes obtained on the controls performed before each practical course (except the introduction course) in order to make sure the students have prepared their practical course. 

- an oral examination, organised the same day as the theoretical examination, aiming to assess how the student masters : 

  • The different techniques used 
  • The significance of obtained results (raw and processed data) 
  • The calculations made on the basis of raw data 
  • Extended interpretation of obtained data.

Any fraud, even regarding the practical courses, will be punished by a 0/20 for the biochemistry course.

 

Sources, references and any support material

Lehninger - Principles of Biochemistry (5th edition) : M. Cox and D.L. Nelson. Chapters 1 to 7, 13 to 16 and 19

Language of instruction

Français
Training Study programme Block Credits Mandatory
Standard 0 5
Standard 2 5