The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results
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 s...
| Main Authors: | , , , |
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| Format: | Article |
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Multidisciplinary Digital Publishing Institute
2019
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| Online Access: | http://hdl.handle.net/1721.1/120465 |
| _version_ | 1826201015080189952 |
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| author | Mallamace, Domenico Fazio, Enza Corsaro, Carmelo Mallamace, Francesco |
| author2 | Massachusetts Institute of Technology. Department of Nuclear Science and Engineering |
| author_facet | Massachusetts Institute of Technology. Department of Nuclear Science and Engineering Mallamace, Domenico Fazio, Enza Corsaro, Carmelo Mallamace, Francesco |
| author_sort | Mallamace, Domenico |
| collection | MIT |
| description | 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 |
| first_indexed | 2024-09-23T11:45:20Z |
| format | Article |
| id | mit-1721.1/120465 |
| institution | Massachusetts Institute of Technology |
| last_indexed | 2024-09-23T11:45:20Z |
| publishDate | 2019 |
| publisher | Multidisciplinary Digital Publishing Institute |
| record_format | dspace |
| spelling | mit-1721.1/1204652022-09-27T21:41:50Z The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results Mallamace, Domenico Fazio, Enza Corsaro, Carmelo Mallamace, Francesco Massachusetts Institute of Technology. Department of Nuclear Science and Engineering Mallamace, Francesco 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 2019-02-15T19:07:29Z 2019-02-15T19:07:29Z 2018-11 2018-10 2019-01-24T09:22:23Z Article http://purl.org/eprint/type/JournalArticle 1422-0067 http://hdl.handle.net/1721.1/120465 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 http://dx.doi.org/10.3390/ijms19123825 International Journal of Molecular Sciences Creative Commons Attribution https://creativecommons.org/licenses/by/4.0/ application/pdf Multidisciplinary Digital Publishing Institute Multidisciplinary Digital Publishing Institute |
| spellingShingle | Mallamace, Domenico Fazio, Enza Corsaro, Carmelo Mallamace, Francesco The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results |
| title | The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results |
| title_full | The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results |
| title_fullStr | The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results |
| title_full_unstemmed | The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results |
| title_short | The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results |
| title_sort | role of hydrogen bonding in the folding unfolding process of hydrated lysozyme a review of recent nmr and ftir results |
| url | http://hdl.handle.net/1721.1/120465 |
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