BMB202: Protein Purification

Study Board of Science

Teaching language: Danish, but English if international students are enrolled
EKA: N220000112, N220000122, N220000102
Censorship: Second examiner: None, Second examiner: External
Grading: Pass/Fail, 7-point grading scale
Offered in: Odense
Offered in: Autumn
Level: PhD

STADS ID (UVA): N220000101
ECTS value: 10

Date of Approval: 29-04-2019


Duration: 1 semester

Version: Approved - active

Comment

The course has limited entry. The following criterias are taken into consideration when seats are assigned.

  1. PhD students after time of enrollment
  2. Students with the most ECTS from their master
  3. Students who follows master courses concurrent with their bachelor programme (dispensation to 30 ECTS Master courses)
If students are equal – seats are allocated based on random draw.
The academic envirometns at The faculty of science manages the prioritisation and at waiting list is established and will then be made aware from the faculty. The waiting list will not be transferred to the following year.

Entry requirements

A Bachelor’s degree in Biochemistry and Molecular Biology, Biomedicine or similar.

Academic preconditions

Students taking the course are expected to:

  • be familiar with basic general and organic chemistry and biochemistry in particular fatty acid metabolism, organic molecular structures and functional groups and pH concept.

  • be familiar with the importance of organic molecules in biochemistry including biological macromolecules.

  • be familiar  with simple inorganic molecules and salts as well as their properties.

  • have practical experience with laboratory work and general laboratory safety.

Participant limit

12

Course introduction

The aim of the course is to enable the student to understand the theory and use of classical protein purification methods and to apply them in practice, which is important in regard to understanding and characterization of protein structure and functions and the development of e.g. protein based drugs.

The course builds on the knowledge acquired in the courses FF503 or similar courses with a focus on general and organic chemistry, BMB532 or similar courses on basic biochemistry and BMB505/536.


In relation to the competence profile of the degree it is the explicit focus of the course to:



  • obtain skills to apply advanced methods to purify and characterize proteins

  • provide skills in creating the experimental basis for the practicality of purification of proteins

  • gain knowledge about the techniques of protein purification and characterization of their properties including enzyme activity.

  • to understand and on a scientific basis reflect on biochemical and molecular biological knowledge, and to identify scientific problems.

Expected learning outcome

The learning objectives of the course is that the student demonstrates the ability to:

  • Discuss and analyze how fatty acid synthesis takes place in bacteria, simple eukaryotic cells like yeast cells, and mammalian cells including various fatty acid synthesis enzyme systems, respectively, in both the cytosol and mitochondria.

  • Discuss the mechanisms behind fatty acid synthesis, elongation and termination

  • Select precise methods for homogenization of specific tissues and cells

  • Evaluate the advantages and disadvantages of ion exchange, gel filtration and affinity chromatography

  • Discuss and analyze the theory behind column chromatography and factors affecting purification and separation of proteins.

  • Discuss the theory of protein solubility and how this may be affected by salt, organic solvents, temperature, and pH.

  • Discuss and analyze the principles of the electrophoretic separation of molecules, including proteins.

  • Discuss and put into perspective the use of electrophoresis in the understanding of protein properties and structure.

  • Discuss and assess typical techniques used for determining the concentration of proteins.

Content

The following main topics are contained in the course:

  • A theoretical part where the theory behind fatty acid synthesis is reviewed.

  • The applied methods used are reviewed.

  • A practical part where a particular protein is purified using the methods above. The methods used include fractionation of cellular components by centrifugation, and protein fractionation by precipitation, ion exchange chromatography and gel filtration chromatography. Furthermore, participants will get to perform photometric determinations of protein and enzyme activities. The purity of the purified protein and its molecular weight is determined by gel electrophoresis.

Literature

  • Robert K, Scopes: Protein Purification - Principles and Practice, Springer Verlag, 3. udgave.
  • Udvalgte forsknings- og oversigtsartikler.

See Blackboard for syllabus lists and additional literature references.

Examination regulations

Prerequisites for participating in the exam a)

Timing

Autumn

Tests

Participation in practical exercises

EKA

N220000112

Censorship

Second examiner: None

Grading

Pass/Fail

Identification

Student Identification Card

Language

Normally, the same as teaching language

Examination aids

To be announced during the course

ECTS value

0

Additional information

The prerequisite examination is a prerequisite for participation in exam element a)

Prerequisites for participating in the exam b)

Timing

Autumn

Tests

Submission of written report

EKA

N220000122

Censorship

Second examiner: None

Grading

Pass/Fail

Identification

Full name and SDU username

Language

Normally, the same as teaching language

Examination aids

To be announced during the course

ECTS value

0

Additional information

The prerequisite examination is a prerequisite for participation in exam element a)

Exam element a)

Timing

Autumn

Prerequisites

Type Prerequisite name Prerequisite course
Examination part Prerequisites for participating in the exam b) N220000101, BMB202: Protein Purification

Tests

Oral examination based on the lab report

EKA

N220000102

Censorship

Second examiner: External

Grading

7-point grading scale

Identification

Student Identification Card

Language

Normally, the same as teaching language

Examination aids

To be announced during the course

ECTS value

10

Additional information

Reexam in the same exam period or immediately thereafter.

The examination form for re-examination may be different from the exam form at the regular exam.

Indicative number of lessons

70 hours per semester

Teaching Method

Activities during the study phase:

  • Self-study of the textbook

  • Written report

  • Individual recap of introductory and training phase

  • Repetition up for the exam

Teacher responsible

Name E-mail Department
Nils J. Færgeman nils.f@bmb.sdu.dk

Timetable

Administrative Unit

Biokemi og Molekylær Biologi

Team at Registration & Legality

NAT

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