Protein Spectroscopy

KBK001F, 3 credits

Valid from: Autumn 2020
Decided by: Senior lecturer Åsa Håkansson
Date of establishment: 2020-06-04

General Information

Division: Pure and Applied Biochemistry
Course type: Third-cycle course
Teaching language: English

Aim

Optical techniques are used to obtain information about the structure, interactions, and dynamics of proteins. It is, therefore, the aim of the course to provide the necessary knowledge to collect “good and reliable” data, to understand preprocessing routines, and eventually to analyze the data.

Goals

Knowledge and Understanding

For a passing grade the doctoral student must

• The student must be able to
• • Understand the different spectroscopy methods that are part of the course. The student should be able to describe the analytical principles and their strength and weaknesses.
• • Understand the different data analysis methods that are part of the course. The student should be able to describe the analysis principles and their strength and weaknesses qualitatively.
• • Besides, the student should understand the importance of sample preparation and sample handling to obtain adequate and reproducible spectroscopic data.

Competences and Skills

For a passing grade the doctoral student must

• • In the context of the spectroscopic characterization of proteins, the student must be able, in a rational way, to choose the adequate method(s) well aware of its strength and weaknesses.
• • Through the tutorials and laboratory exercises the student would have gained certain experimental experience and data processing and interpretation knowledge.

Judgement and Approach

For a passing grade the doctoral student must

• The student must be able to
• • Discuss the adequateness of the methodologies used in the scientific literature concerned.
• • Compare and integrate results from different characterization methods.

Course Contents

The course consists of compulsory lectures, tutorials, lab practicals, and presentations. The week of study is articulated as follows: - Short description of the techniques and what they can do - Short description of advanced usages of the techniques and analysis (accessories and software) - Short description and tutorial on data analysis, especially secondary structure estimation and conformational transitions - Lab practicals with all four techniques on standard proteins and students' proteins (data collection and analysis).

Course Literature

The literature is provided as a compilation of scientific articles and reviews

Instruction Details

Types of instruction: Lectures, laboratory exercises, exercises. The course consists of 1 intensive week of lectures, tutorial, lab practicals, and student oral presentation. Besides, the student is invited to discuss her/his research challenges.

Examination Details

Examination format: Seminars given by participants. Assessment: compulsory presence (80%), participation in tutorials, lab practicals, and oral presentation.
Grading scale: Failed, pass
Examiner:

Admission Details

Admission requirements: Enrolled in a doctoral study involving biomacromolecules
Assumed prior knowledge: Basic knowledge in protein primary and secondary structure
Selection criteria: The course is limited to a maximum of 8 students. The selection will be on the first come first serve basis.

Course Occasion Information

Contact and Other Information

Course coordinators: