Abstract
The importance of the flexibility of a protein molecule (“the fourth dimension”) for the proper functioning of the protein can not be over-estimated. One of the most potent methods to study the motility of protein structure is the detection of peptide NH H-exchange [1,2]. The approach is based on the notion that protons are accessible for the solvent catalysts (OH- and H3O+) which cause exchange only if the H-bond the proton is involved in is broken. There are several models describing processes which bring about breakage of intramolecular H-bonds [3]. It has been proposed long ago to use H-D exchange sensitive IR bands to elucidate the flexibility of proteins [4]. Recently we studied extensively H-D exchange processes in several proteins (among them proteins which can not been tuned through the phase transition reversibly) under conditions of a steady and sudden heating of the enzyme solution.
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References
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© 1995 Springer Science+Business Media Dordrecht
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Backmann, J., Fabian, H., Naumann, D. (1995). The Thermally Induced Hydrogen Exchange in Different Proteins as Seen by FTIR Spectroscopy. In: Merlin, J.C., Turrell, S., Huvenne, J.P. (eds) Spectroscopy of Biological Molecules. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-0371-8_47
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DOI: https://doi.org/10.1007/978-94-011-0371-8_47
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