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Institutionernas kurser för doktorander

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Kursplan för

Läsår
KBB056 - Structural biochemistry
 
Kursplanen fastställd 2010-02-23 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: D

Modul   Poängfördelning   Tentamensdatum
Lp1 Lp2 Lp3 Lp4 Sommarkurs Ej Lp
0105 Tentamen 7,5 hp Betygskala: TH   7,5 hp   20 Dec 2012 fm V,  02 Apr 2013 fm V

I program

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

Examinator:

Professor  Richard Neutze


Ersätter

KBB055   Strukturbiokemi

Kursutvärdering:

http://document.chalmers.se/doc/4ff8bdf1-0982-4210-84ad-0fb03dd2b36a


Behörighet:

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

Kursspecifika förkunskaper

Anyone at fourth year within the Bt or K programmes at Chalmers will automatically be accepted. The course will have a significant mathematical component.

Syfte

This course aims to provide an understanding of the major methods for structure determination of proteins. The course will cover X-ray crystallography and Nuclear Magnetic Resonance Spectroscopy in detail, and Electron Paramagnetic Resonance and Electron Microscopy in less detail. Students will be expected to understand the steps required to solve a protien structure, and the physical concepts which underpin these methods.

Lärandemål (efter fullgjord kurs ska studenten kunna)

At the completion of this course students will be able to set up crystallisation drops, process X-ray diffraction data (using Mosflm), visualise protein structures and electron density (using COOT), assign NMR spectra and interpret these in terms of structure.

Innehåll

The course will consist of lectures and laboratory assignments. Lectures will run for two hours three times a week & will cover space groups; X-ray diffraction theory; NMR spectroscopy theory; Electron microscopy theory; and several examples of protein structures and methods. Inter-dispersed within the lecture course will be the occasional tutorial where specific problems will be worked through. Laboratory exercises will run for one afternoon over seven weeks and are compulsory. They will consist of X-ray crystallisation & data collection, model building & structure analysis, and NMR spectroscopy.

Organisation

This course consists of up to 30 two hour lectures (including tutorials) and seven laboratory assignments.


Lectures will run for two hours almost every day & will cover protein crystallisation and space groups; X-ray diffraction theory; Nuclear Magnetic Resonance spectroscopy theory; Electron Paramagnetic Resonance spectroscopy theory; and will provide a number of examples where X-ray and NMR methods have been used to solve protein structures.


There will be a total of seven Laboratory exercises which will run for one afternoon each. These compulsory laboratory exercises are an extremely valuable part of the course and consist of X-ray crystallisation, Fourier Transforms, X-ray diffraction data analysis, Structural model building, & structure analysis, and NMR spectral assignment, and NMR structural modelling, and EPR spectroscopy.

Litteratur

Two useful (but not compulsory) texts are:


"Molecular Methods in Biophysics: Structure, Dynamics, Function" by Serdyuk, Zaccai & Zaccai "Crystallography made crystal clear: a guide for users of macromolecular models" by Rhodes


The course schedule and lecture notes will be placed on the homepage http://www.csb.gu.se/neutze/structure/


 

Examination

Course grades will be awarded upon the performance in a written exam. Laboratory exercises must also be performed to a suitable level to recieve credit.


 


Sidansvarig Publicerad: må 13 jul 2020.