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.

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

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

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.

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

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.

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

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.

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

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.

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.