Learning outcomes

Familiarize the student with the three-dimensional (3D) structure of proteins, the experimental determination of this 3D structure as well as the methods of predicting the 3D structure. Protein manipulation (protein engineering) will also be addressed, using examples from the literature and/or external speakers.

Goals

At the end of the course, students will master the concepts related to the structure of a biological macromolecule, be able to critically understand a scientific article, and be able to synthesize and present results.

Content

The course will consist of:

- a section on experimental techniques for determining the structure of biological macromolecules,

- a section on theoretical approaches to modelling biological macromolecules.

 

In addition to a set of theoretical concepts, a practical application will be offered in the form of a tutorial(s). A report will be submitted on a date set by the teachers and will serve as the basis for the examination.

Table of contents

- Brief description of the topics covered

Physical interactions within proteins and energy contributions that allow the folding and stability of the folded structure of biological macromolecules. Concepts such as "force fields" will also be discussed.

Experimental techniques for determining the structure of biological macromolecules. Physicochemical methods can be used to propose a model of the three-dimensional structure of a protein. These methods include X-ray diffraction on protein crystals and nuclear magnetic resonance. Other approaches, such as fluorescence and circular dichroism, can also characterize the structure of a protein.

Theoretical approaches for modelling biological macromolecules

Assessment method

The evaluation is based on the performance and defence of a work.

Sources, references and any support material

see webcampus

Language of instruction

Français