The specific structure of a protein is stabilized by numerous hydrogen bonds that connect individual amino acids. Using an innovative method, namely Nuclear Magnetic Resonance (NMR) spectroscopy in combination with high pressure, Dr. Nisius and Prof. Grzesiek from the Biozentrum of the University of Basel have provided important new insights into the hydrogen bond network of Ubiquitin and its importance for the stability of this model protein. Their findings have now been published in the renowned scientific journal Nature Chemistry.
Under pressure: scientists investigate hydrogen bonds under pressures of up to 2500 bar
Proteins consist of a sequence of amino acids and have important physiological functions, such as catalysis or transport of metabolic products. To perform their physiological role, proteins need to fold their linear amino acid chains into a stable three-dimensional structure. In part, the spatial arrangement is determined by a network of hydrogen bonds. However so far it was unclear to what extent individual hydrogen bonds contribute to the stability of a structure. Using a newly developed high pressure cell and NMR method Dr. Nisius and Prof. Grzesiek could, for the first time, completely characterize the stability of individual hydrogen bonds in the protein Ubiquitin.Particular stability of key, long-range hydrogen bonds
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