Goals and Learning Outcomes

Overall goal

The main goal is to provide the student with basic knowledge and insight about the three-dimensional (3D) structure of macromolecules (protein and nucleic acids) and the relationship between structure and function. A general introduction to determination of 3D structure is included.

Teaching is based on a knowledge-interaction concept that is used to increase and deepen the perception and understanding of 3D structure and structure-function relationships.

To achieve this, lectures are intimately coupled to interactive computer exercises known as kinetic images (kinemages) where structures are studied and analyzed in 3D.

At the end of this course, you will have arrived at a better understanding of the basic properties of protein structure. Your way of knowing protein structure has changed from the typical 2D view (the over-simplified presentation of amino acids, secondary structure and tertiary structure provided in regular text books) to the more useful 3D perception.

The structure of a certain protein or nucleic acid has become intimately coupled to its respective function. You will know the basic principles of 3D structure determination and validation.

Specific goals

You should be able to describe the main characteristics of amino acids and and the principle types of motifs and folds.

You should know about the principle forces that fold the proteins and maintain the structures, and be able to suggest changes to a protein structure that would lead to for instance increased thermostability.

You should be able to describe the function of a number of important proteins and relate function to the structure.

With the aid of kinemage exercises, you should be able to relate information from the course literature to the actual 3D structures.

You should know about the functions and tools available in the structure database, and be able to use these for retrieving information and structures, as well as validating structures.

You should be able to validate a 3D structure using tools available in the structure database and by analyzing electron-density maps.

You should be able to outline the principles for crystallization of soluble, globular proteins.

You should know the basic principles for how a 3D structure is determined, most importantly using the method of X-ray crystallography.

During the seminar project, you will study in detail a specific protein structure and its function. Guided by information retrieved from the course and scientific articles, you should be able to analyze, validate and discuss the structure, and to present your observations and reflections as a written report as well as an oral presentation at the end of the course.

Requirements

One written examination (TEN 1; 4 hp, grades A-F), laboratory course (LAB1; 1.5 hp, grades Pass/Fail) and literature task (LIT1; 2.0 hp, grades Pass/Fail)