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Review

The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results

1
Dipartimento di Scienze Matematiche e Informatiche, Scienze Fisiche e Scienze della Terra (MIFT), Università di Messina, 98166 Messina, Italy
2
Department of Nuclear Science and Engineering, Massachusetts Institute of Technology (MIT), Cambridge, MA 02139, USA
3
Istituto dei Sistemi Complessi (ISC)—CNR, 00185 Rome, Italy
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2018, 19(12), 3825; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms19123825
Received: 31 October 2018 / Revised: 23 November 2018 / Accepted: 24 November 2018 / Published: 30 November 2018
(This article belongs to the Collection Protein Folding)
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. View Full-Text
Keywords: protein denaturation; FTIR; NMR; hydration water; hydrogen bonding; energy landscape protein denaturation; FTIR; NMR; hydration water; hydrogen bonding; energy landscape
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MDPI and ACS Style

Mallamace, D.; Fazio, E.; Mallamace, F.; Corsaro, C. The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results. Int. J. Mol. Sci. 2018, 19, 3825. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms19123825

AMA Style

Mallamace D, Fazio E, Mallamace F, Corsaro C. 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. 2018; 19(12):3825. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms19123825

Chicago/Turabian Style

Mallamace, Domenico, Enza Fazio, Francesco Mallamace, and Carmelo Corsaro. 2018. "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, no. 12: 3825. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms19123825

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