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Project 7

NMR Investigations of Biocatalysed Reactions

Supervisor: Prof. Lothar Brecker

Student: Markus Husa

A large number of NMR methods has already been established for the determination of enzyme structures. One of the most common techniques to calculate solution state, primary, secondary, tertiary and even quartery structures of proteins is based upon the sequential assigment of proton and carbon signals by multidimensional NMR techniques. Consequently, spatial interactions of assigned signals are measured and possible structures calculated.

In the present work the focus of attention is put mainly on the binding of substrates and products as well as on the structure of the active site. Therefore, the arduous labor of complete assignment of a protein’s signals can be avoided, the resulting spectra are simplified and time efficiency is ensured. All of the methods outlined in the following rely on short residence times of the substrate in the active center, immediate spatial proximity and large resultant spin-spin interactions of high-gamma nuclei of enzyme and substrate, respectively.

Initiativkolleg Functional Molecules
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