The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results
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ijms-19-03825.pdf
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Author(s)
Mallamace, Domenico
Fazio, Enza
Corsaro, Carmelo
Mallamace, Francesco
Date Issued
November 2018
Journal
International Journal of Molecular Sciences
Publisher
Multidisciplinary Digital Publishing Institute
Citation
Mallamace, Domenico et al. "The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results." International Journal of Molecular Sciences 19, 12 (November 2018): 3825 © 2018 The Authors
Version
Final published version
Abstract
The biological activity of proteins depends on their three-dimensional structure, known as the native state. The main force driving the correct folding mechanism is the hydrophobic effect and when this folding kinetics is altered, aggregation phenomena intervene causing the occurrence of illnesses such as Alzheimer and Parkinson’s diseases. The other important effect is performed by water molecules and by their ability to form a complex network of hydrogen bonds whose dynamics influence the mobility of protein amino acids. In this work, we review the recent results obtained by means of spectroscopic techniques, such as Fourier Transform Infrared (FTIR) and Nuclear Magnetic Resonance (NMR) spectroscopies, on hydrated lysozyme. In particular, we explore the Energy Landscape from the thermal region of configurational stability up to that of the irreversible denaturation. The importance of the coupling between the solute and the solvent will be highlighted as well as the different behaviors of hydrophilic and hydrophobic moieties of protein amino acid residues. Keywords: protein denaturation; FTIR; NMR; hydration water; hydrogen bonding; energy landscape
MIT Department
Massachusetts Institute of Technology. Department of Nuclear Science and Engineering
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Creative Commons Attribution
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DOI of Published Version
https://doi.org/10.3390/ijms19123825
