Doctoral Studies

Biomolecular Chemistry - Field

Topic name: Optimized NMR Experiments for Large Biomolecules

Supervisor: doc. RNDr. Radovan Fiala, CSc.

Předběžné zadání:
In NMR spectroscopy, the factors limiting the studies of large biomolecules (Mw larger than approx. 150,000) are a high number of signals in spectra causing their overlap and the diminishing sensitivity caused by fast relaxation processes. Several methods have been proposed to overcome these limitations. The problem of resolution can be addressed by increasing the number of dimensions in the spectra. To make the experiments with more than three dimensions practically feasible, nonlinear sampling techniques and projection reconstruction methods in a combination with fast acquisition schemes (SOFAST-NMR) have been applied. The sensitivity can be improved by selecting the slow-relaxing components of magnetization as in the TROSY (Transverse Relaxation Optimized SpectroscopY). The progress in the probe technology allows direct detection of C-13 signal at concentrations typical for the solutions of biomolecules. By combining the above mentioned approaches, NMR spectra of proteins and nucleic acids can be obtained with better resolution and sensitivity. The task is to propose such experiments, optimize their performance, and prove their usefulness by measuring the spectra of selected samples studied in the laboratory.
CAVANAGH, John. Protein NMR spectroscopy :principles and practice. 2nd ed. Amsterdam: Elsevier, 2007. xxv, 885. ISBN 9780121644918.

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