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Institutionernas kurser för doktorander

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Kursplan för

Läsår
KBB110 - Protein engineering 1
 
Kursplanen fastställd 2011-02-20 av programansvarig (eller motsvarande)
Ägare: MPBIO
7,5 Poäng
Betygskala: TH - Fem, Fyra, Tre, Underkänt
Utbildningsnivå: Avancerad nivå
Huvudområde: Bioteknik, Kemiteknik
Institution: 0346 - KEMI GU


Undervisningsspråk: Engelska
Blockschema: B

Modul   Poängfördelning   Tentamensdatum
Lp1 Lp2 Lp3 Lp4 Sommarkurs Ej Lp
0107 Tentamen 7,5 hp Betygskala: TH   7,5 hp   15 Mar 2013 em V,  Kontakta examinator,  28 Aug 2013 fm V

I program

MPBIO BIOTECHNOLOGY, MSC PROGR, Årskurs 2 (valbar)
MPBIO BIOTECHNOLOGY, MSC PROGR, Årskurs 1 (obligatoriskt valbar)

Examinator:

Professor  Jan Rydström


Ersätter

KBB095   Genteknisk proteinmodellering

Kursutvärdering:

http://document.chalmers.se/doc/01adc839-014d-4577-8c2b-8de0b4ab5b5a


Behörighet:

För kurser inom Chalmers utbildningsprogram gäller samma behörighetskrav som till de(t) program kursen ingår i.

Kursspecifika förkunskaper

Undergraduate profile: Major in Bioengineering, Chemistry or Chemical engineering
Prerequisites: Chemistry and biochemistry, Cell and molecular biology

Syfte

The aim of the course is to solve a structure-function problem in a protein, based on a known amino acid sequence and possibly 3D-structure, by using site-specific mutagenesis, followed by expression of the mutant protein, purification and biochemical and functional characterization. This strategy gives an in-depth insight into structure-function relationships of proteins. The course is suitable for students interested in research/Ph.D. training, the pharmaceutical- or food industry, or other biotechnology-oriented industry.

Lärandemål (efter fullgjord kurs ska studenten kunna)

After completion of this course, the student should be able to


 



  • In practical terms, carry out site-specific mutagenesis, i.e. based on a known amino acid sequence, replace an amino acid in a soluble protein or membrane protein, produce the mutant gene by PCR, and sequence the gene.

  • Express the mutated gene to a protein in a suitable prokaryotic or eukaryotic (yeast) expression system, and learn other both proaryotic and eukaryotic expression systems, their advantages and disadvantages.

  • Control which factors that determine yield and correct folding of the protein, and methods which limit the ocurrence of inclusion bodies.

  • Purify the protein to near homgeneity by chromatographic techniques, and methods to demonstrate the purity of the preparation, e.g polyacrylamide gel electrophoresis, as well as other methods.

  • Apply alternative methods for expression, e.g. in vitro expression using a cell-free system.

  • Apply selected aspects of protein engineering in an industrial environment

Innehåll

The course is research-oriented and designed to show how modern molecular and biochemical methods can be combined and used in order to specifically predict and test structure-function relationships in proteins, a strategy which often is used in biomedical research and the biotechnology industry. This is achieved by carrying out the entire process, from the identification of a structure-function problem in a protein, to the mutation of the gene coding for the protein, and the expression, purification and characterization of the protein. The target protein can be either a soluble protein or a membrane protein. All steps are carried out by the student, who therefore will learn all critical stages in this process and several valuable methods in protein chemistry, and evaluate functional changes caused by mutagenesis. Since all mutations are unique, i.e. they have not been done previously, the results can sometimes be published.


The course contains the following parts:
Basic materials science:
Identification of a suitable amino acid in a protein for mutagenesis
Mutagenesis and PCR
Expression of a gene in a prokaryot and/or eukaryot expression system
Isolation and purification of the expressed protein
Application of various types of chromatographic purification systems
Characterization of the purified protein regarding purity and function

Organisation

The course includes about 20 lectures (2x45 min), and extensive laboratory exercises.

Litteratur

Principles and Techniques of Biochemistry and Molecular Biology, ed. av Keith Wilson & John Walker, 7th edition, Cambridge University Press, 2005.

Examination

The examination is based on a written exam, grades TH, and approved laboratory exercises and reports.


Sidansvarig Publicerad: må 13 jul 2020.