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Graduate courses

Departments' graduate courses for PhD-students.

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Syllabus for

Academic year
KBB111 - Design and production of biomolecules
Design och produktion av biomolekyler
 
Syllabus adopted 2019-02-12 by Head of Programme (or corresponding)
Owner: MPBIO
7,5 Credits
Grading: TH - Five, Four, Three, Fail
Education cycle: Second-cycle
Major subject: Bioengineering, Chemical Engineering
Department: 0114 - KEMI OCH MOLEKYLÄRBIOLOGI GU


Teaching language: English
Application code: 08119
Open for exchange students: No
Maximum participants: 40

Module   Credit distribution   Examination dates
Sp1 Sp2 Sp3 Sp4 Summer course No Sp
0114 Laboratory 2,5c Grading: UG   2,5c    
0214 Examination 5,0c Grading: TH   5,0c   Contact examiner,  Contact examiner,  Contact examiner

In programs

MPBIO BIOTECHNOLOGY, MSC PROGR, Year 1 (compulsory elective)
MPBIO BIOTECHNOLOGY, MSC PROGR, Year 2 (elective)

Examiner:

Kristina Hedfalk

  Go to Course Homepage

Replaces

KBB110   Protein engineering 1


Eligibility:


In order to be eligible for a second cycle course the applicant needs to fulfil the general and specific entry requirements of the programme that owns the course. (If the second cycle course is owned by a first cycle programme, second cycle entry requirements apply.)
Exemption from the eligibility requirement: Applicants enrolled in a programme at Chalmers where the course is included in the study programme are exempted from fulfilling these requirements.

Course specific prerequisites

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

Aim

The aim of the course is to give a deep understanding of the structure-function relationship of proteins coupled to the production and purification of selected targets. Primarily we focus on membrane bound proteins which constitute the majority of the target molecules of current drugs.To illustrate the questions and the methodology presented on the lectures a number of laboratory exercises are included which are tightly linked to present research. The course is given by the Department of Chemistry and Molecular Biology at the University of Gothenburg and it is suitable for students interested in a master project in Biochemistry or a future job directed towards research, food or biotechnology within research or industry.

Learning outcomes (after completion of the course the student should be able to)

The theoretical and laboratory parts of the cource are tighly connected to ongoing research and the aim is to prepare the students for a master project in biochemistry or for continued research studies in the subject. By passing the course the student is supposed to be able to:

Knowledge and understanding

- describe the general structure-function relationship of proteins on a deeper level

- describe methods for expression, purification and characterization of soluble as well as membrane bound proteins

- describe the most common methods in spectroscopy (absorption of visible and UV light as well as fluorescence) used for protein characterization

- describe the theoretical and practical enzyme kinetics applied on reactions having multiple substrates

- describe the principles for membrane transport catalyzed by membrane proteins as well as giving specific examples

- describe the mechanism behind signal transduction and interpretation of sensory information provided by proteins

- describe how proteins act as molecular motors

Competence and ability

- plan and design a biochemical project

- apply methods for expression, purification and characterization of soluble as well as membrane bound proteins

- to some extent apply the most common spectroscopic methods (absorption of visible and UV light and fluorescence) for characterization of proteins

- suggest and motivate suitable mutations for characterization of protein stability, structure and/or function

- design a cloning experiments as well as primers for PCR

- independently follow an experimental protocol

- present an experimental result in a written report in an adequate and understandable way

Ability to assess and approach

- interpret and discuss experimental results as well as to draw proper conclusions

- draw conclusions concerning the effect of a certain mutation on the properties of the protein

- reflect on the application of protein design from a socially perspective

Content

Designed proteins have a broad occurence in our modern society and they are important for fundamental research, production of drugs as well as in food industry. Many molecules are difficult to produce and study wher the process can be simplified with assistance from intentional design of the target protein, a method which constitute an essential building block in biochemistry of today. This course gives enhanced knowledge in directed mutagenesis and recombinant DNA technology, production of proteins in various host systems as well as in the structure and function of proteins. The course can be divided in two sub courses: one theoretical and one practical.

Sub course 1: Design and production of biomolecules, theory, 5 hec

The theoretical sub course gives an enhanced knowledge in the involvement of proteins in the transport over the membrane, signal transduction, the mediation of our five senses and how they function as molecular motors. In addition, the theory behind the methods applied in sub course 2 is covered as well as practical applications and the project planning of those. Those topics are brought up in the form of lectures as well as in an exercise dealing with the formulation of a project plan.

Sub course 2: Advanced biochemical methodology and analysis, 2,5 hec

Through laboratory exercises, the practical sub course gives enhanced knowledge about methodologies for production, separation, purification and characterization of proteins. The following methods are applied among others: protein design and protein production, electrophoresis, chromatography, spectroscopy and enzyme kinetics.


Organisation

The course is provided by the Department of chemistry and molecular biology at the University of Gothenburg and the schedule is, as far as possible, adapted to parallel courses at Chalmers University of Technology. The course includes up to 20 lectures (2x45 min) where invited lecturers from academia and industry contribute to cover various aspects within advanced Biochemistry. An important part of the course is the laboratory exercise which give insight into key steps in the process from protein design to final characterization of the pure protein product. 

Literature

Berg, J. M., Tymoczko, John L., & Stryer, Lubert,. (2012). Biochemistry. (7. ed., International ed.). Basingstoke: Palgrave Macmillan.

Wilson, K. (Ed.). (2010). Principles and techniques of biochemistry and molecular biology. (7. ed.). Cambridge: Cambridge University Press.


Examination including compulsory elements

The obligatory parts of the course are the laboratory exercises and the written laboratory report. The goal of the course are examined through a written exam at the end of the course, written laboratory reports and a practical laboratory examination. 



Published: Wed 26 Feb 2020.