This page is printed on Jun 29, 2017 from http://www.bionmr.chem.au.dk/bionmr/education/index.php

 
 

B12/PhCh 411: Solid-State NMR Spectroscopy

Content:

The course aims at giving the participants a fundamental knowledge of the theory of and practical experiments in modern solid-state NMR spectroscopy and its applications. The course provides an introduction to the general theory relevant for the understanding and description of advanced multiple-pulse NMR experiments, anisotropic nuclear spin interactions, and computer simulation of solid-state NMR experiments and spectra. The lectures and theoretical exercises will be supplemented by practical applications on our solid-state NMR spectrometers.

Textbooks:

N. C. Nielsen: Forelęsningsnoter i Faststof NMR Spektroskopi. Introduktion til Beregning af Faststof NMR Spektre.

Requirements:

Basic NMR (Kemi A6) and computation (datK) or similar is an advantage but not required.

Education form: 6 hours of lectures/exercises per week.
Examination: Pass/fall on basis of obligatory exercises.
Credits:2 points of 10 ECTS credits.
Semester:Spring
Teachers:Niels Chr. Nielsen, Thomas Vosegaard.
Comments:The course requires at least 3 and maximum 12 participants.

B29/PhCh 419: Biomolecular NMR Spectroscopy

Content:

The course aims at giving the participants a fundamental knowledge of the theory of and the practical experiments in modeter biological liquid-state NMR spectroscopy and its applications to protein structure determination.

Textbooks:

J. Cavanagh, W. J. Fairbrother, A. G. Palmer III, and N. J. Skelton: Protein NMR Spectroscopy. Principles and Practice, Academic Press, 1996.

Requirements: Part 1 of the chemistry or biotechnology education or similar.
Education form: 4 hours of lectures/exercises per week. Student seminars.
Examination: Pass/fall on basis of obligatory exercises/seminars.
Credits:2 points of 10 ECTS credits.
Semester:Fall.
Teachers:Niels Chr. Nielsen, Anders Malmendal.
Comments:The course requires at least 3 participants.

Physical Biochemistry

Content:

The course provides a basic introduction to the principles behind and the application of various physcial measuring methods. This includes chromatography (HPLC, FPLC), various spectrosocpies (UV, IR, CD, fluoresence, NMR, EPR), spectrometry (MS), diffraction (XRD), microscopy (EM, confocal), imaging (MR), electrophoresis and caliometry. Priority is given to a coherent and comparative description and the general application of the methods to obtain complentary information about biological molelcules.

Textbook:

Principles of Physical Biochemistry, Kensal E. van Holde, W. Curtis Johnson, and P. Shing Ho, Prentice Hall, NJ 1998.

Requirements: One year study in molecular biology or chemistry.
Education Form: 3F + 3TŲ per week.
Examination: 4 hours written examination.
Credits:10 ECTS points.
Semester:Fall.
Teachers:Niels Chr. Nielsen, Anders Malmendal, Thomas Vosegaard, Lars Sottrup-Jensen.
Homepage:Fysisk biokemi 1 and Fysisk biokemi 2

Ph.D course in protein structure

Content:

A course in determination and analysis of protein structures will be held yearly in the second-last week of August (August 9 to 13, 2004) at Science Park Århus. The course will include X-ray analysis, NMR spectroscopy, electron- and confocal microscopy, mass spectroscopy, surface plasmon resonance, calorimetry, cicular dichroism, atomic force microscopy, scanning tunneling microscopy, small-angle X-ray scattering, molecular modelling, and structure prediction. The purpose of the course is to introduce the students to the major techniques available for describing structural/functional relationships in proteins.

The course is limited to persons who are enrolled as Ph.D.-students and will be free of charge. All expenses covering accommodation, meals and travel must be paid by the participants. Students who want to participate in the course must register using the registration entry in homepage, below. The number of participants is limited so the organizers might have to select among applicants. Further information can be obtained by contacting Prof. Niels Chr. Nielsen (Phone +45-89423841, E-mail ncn@chem.au.dk, fax +45-86196199).
Programme.

Textbooks:Notes, articles etc.
Requirements: Enrolled Ph.D. student
Education form: 1 week containing seminars, exercises etc.
Examination: None. Active participation in full course.
Credits: 1 point. 5 ECTS credits.
Semester:August 9-13, 2004
Teachers:

Peter Andreasen, Arvid B. Maunsbach, Søren K. Moestrup, Niels C. Nielsen, Jens Nyborg, Torben E. Petersen, and Søren S. Thirup plus invited guest speakers.

Comments:Limited number of participants. Application.

B course: Protein structure and function

Content:

This course contains the description of the general structure of proteins, polysaccharides and nucleic acids as well as their conformation and folding. The chemical and physical properties wich are of importance for the structure and interactions of these macromolescules will be studied. The properties of macromolecules in solution and their interactions in solution and in crystals are described.

The structure and function of examples from essential areas of biochemistry will be enlightened by the use of PC based display programmes during computer exercises. Possible examples will be enzymatic reactions, proteolytic enzymes and their inhibitors, immunoglobulins, vira, binding of nucleotides, protein/nucleic acid complexes, control of transscription, DNA and RNA.

We will present the NMR part of the module Detailed programme.

Textbooks:

T. E. Creighton: Proteins: Structures and molecular properties, Second Ed., Freeman and Company, 1993. C. Branden and J. Tooze, Introduction to protein structure, 2nd Ed., Garland Publishing, 1998.

Requirements:
Education form:
Examination:Written examination (13-scale).
Credits:10 ECTS credits
Semester:Spring semester.
Teachers:Lars Sottrup-Jensen, Jens Nyborg, Niels C. Nielsen, Lasse Jenner.
Comments:

Journal club/local seminars

For education and competence development purposes the group have a one hour meeting every week with presentation of own results or important new topics in the literature within the area of biomolecular solid-state and solution NMR. The specific topics can be found under the local entry of our homepage.

Graduate and Ph.D. projects in Biomolecular NMR (in Danish)

Laboratorium for biomolekylær NMR spektroskopi er en forskningsenhed ved Kemisk Institut, der varetager forskning inden for udvikling og anvendelse af NMR spektroskopi til bestemmelse af stuktur og dynamik for biologiske makromolekyler. I løbet af år 2003-2004 er NMR aktiviteten gradvist blevet overført til egne laboratorier med 400 og 700 MHz spektrometre optimalt udstyret til multidimensionel/multikerne biomolekylær væske- og faststof NMR, ligesom der er foretaget etablering af kemi- og computer laboratorier samt udbygning af den videnskabelige kapacitet i gruppen.

Forskningsaktiviteten ved Laboratorium for Biomolekylær NMR spektroskopi er centreret omkring bestemmelse af struktur og dynamik for biologiske makromolekyler herunder specielt membran proteiner (eksempelvis ion/vand kanaler), protein-"assemblies"/polymerer, ligand-receptor interaktioner, aktive metal "binding-sites" og biomineralisering. Den overordnede målsætning er studie af struktur-funktion sammenhænge. Hertil anvendes kombination af væskefase NMR spektroskopi til bestemmelse af højtopløste tre-dimensionelle strukturer af proteiner/nukleinsyrer i standard eller detergent opløsning samt faststof NMR spektroskopi til bestemmelse af struktur og konformation af f.eks. membran-associerede proteiner/peptider (opløsning i phospholipid bilagsmembraner). I forbindelse med begge typer NMR spektroskopi udvikles og implementeres nye eksperimentelle metoder til optimal opnåelse af specifik strukturel information.

Med udgangspunkt i kombinationen mellem faststof og væskefase NMR spektroskopi samt mellem anvendelse og metodeudvikling bliver studerende ved Laboratorium for Biomolekylær NMR spektroskopi uddannet inden for et bredt spektrum af faglige dicipliner rækkende fra molekylær biologi via kemi og avanceret kvantefysik til numerisk beregning og datalogi. Afhængig af interesse og eventuelt engagement i samarbejdsprojekter med inden- og udenlandske samarbejdspartnere (læreanstalter eller industri) kan speciale- og Ph.D. projekter typisk involvere en passende kombination af disse dicipliner. Netop dette forhold har været medvirkende til, (i) at de studerende i høj grad har været i stand til at tilrettelægge deres forskningprojekter til opfyldelse af egne interesser og (ii) at tidligere studenter fra afdelingen har fået jobs ved uden- og indenlandske forskningslaboratorier og industrivirksomheder inden for f.eks. NMR/MR, datalogi og ingeniør virksomhed. Et typisk speciale- eller Ph.D. projekt vil i den indledende fase involvere grundforskning i tilknytning til laboratoriets primære aktiviteter og vil således involvere samarbejde med en del af gruppens øvrige medarbejdere og studerende. Under studiet motiveres den studerende til stigende grad af engagement, ansvar og selvstændighed i udførelsen af projekter. Udover deciderede projektaktiviteter vil uddannelsen involvere præsentation af resultater ved artikelskrivning og foredrag samt rejser til internationale konferencer og besøg/ophold i andre forskningslaboratorier. Der er i øjeblikket tilknyttet 4 ph.d. og 4 speciale studerende til laboratoriet. Der er ledige speciale- og ph.d. uddannelse pladser i tilknytning til Laboratorium for Biomolekylær NMR Spektroskopi med relationer til de naturvidenskabelige og medicinske fakulteter ved Aarhus Universitet.