BB2160 Structure Biology 7.5 credits

• Educational level

  Second cycle

• Academic level (A-D)

  D

• Subject area

  Biotechnology
  

• Grade scale

  A, B, C, D, E, FX, F

• Homepage of the Course

• Course page on KTH Social

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 the determination of 3D structure is included. The 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. 

Specific aims 

You should be able to describe the main characteristics of amino acids 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 their function to the structure. With the aid of kinemage exercises, you should be able to draw connections between the information from the course literature and 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.

Course main content

Biomolecular structures. High resolution structure detemination techniques such as NMR-spectroscopy and X-ray crystallography. Forces that fold the proteins and maintain the structures. Structure-function relationship examples e.g. transcription factors, immunoglobulines, and signal transduction proteins. Structural databases, visualization and analysis of structures. Applications in pharmaceutical industry.

Eligibility

Admission requirements for independent students:
A total of 20 university credits (hp) in biochemistry, microbiology and gene technology/molecular biology. 30 university credits (hp)  chemistry, as well as 20 university credits (hp) in mathematics and computer science or corresponding. Documented proficiency in English corresponding to English B.

Admission requirements for programme students at KTH:

Prerequisites

SF1633 Differential Equations I, KD1060 Molecular Structure and BB1010 Introduction to Biotechnology.

Literature

Branden C, and Tooze J., Introduction to Protein Structure, 2nd Ed. Garland Publishing Inc., 1999, and relevant handouts

Examination

• LAB1 - Laboratory Work, 1.5 credits, grade scale: P, F
• LIT1 - Literature Task, 2.0 credits, grade scale: P, F
• TEN1 - Examination, 4.0 credits, grade scale: A, B, C, D, E, FX, F

Requirements for final grade

Examination (TEN 1; 4,0 credits, grading scale A - F), Laboratory Course (LAB1; 1,5 credits, grading scale Pass/Fail)
Literature assignment (LIT1; 2,0 credits, grading scale A-F).

Offered by

BIO/Biotechnology

Examiner

Christina Divne <divne@kth.se>

Supplementary information

Students are required to sign up at least two weeks in advance for examination.

The course is given provided at least seven students are admitted.

Version

Course plan valid from: Spring 11.
Examination information valid from: Autumn 07.