ArticleComputational and structural biotechnology journal2015
The role of water in protein's behavior: The two dynamical crossovers studied by NMR and FTIR techniques.
Article in Computational and structural biotechnology journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
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- Cholesterol Changes Interfacial Water Alignment in Model Cell Membranes.Journal of the American Chemical Society · 2024Article
- Redefining vascular repair: revealing cellular responses on PEUU-gelatin electrospun vascular grafts for endothelialization and immune responses onFrontiers in bioengineering and biotechnology · 2024Article
- Co-Gelation of Pumpkin-Seed Protein with Egg-White Protein.Foods (Basel, Switzerland) · 2023Article
- Dentin primer based on a highly functionalized gelatin-methacryloyl hydrogel.Dental materials : official publication of the Academy of Dental Materials · 2023Article
- In-line monitoring of protein concentration with MIR spectroscopy during UFDF.Engineering in life sciences · 2023Article
- Development of a Multi-Enzymatic Biocatalytic System through Immobilization on High Quality Few-Layer bio-Graphene.Nanomaterials (Basel, Switzerland) · 2022Article
- Lysozyme microspheres incorporated with anisotropic gold nanorods for ultrasound activated drug delivery.Ultrasonics sonochemistry · 2022Article
- Combining a Genetically Engineered Oxidase with Hydrogen-Bonded Organic Frameworks (HOFs) for Highly Efficient Biocomposites.Angewandte Chemie (International ed. in English) · 2022Article
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Authors and funding
6 authors.
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Abstract
The role the solvent plays in determining the biological activity of proteins is of primary importance. Water is the solvent of life and proteins need at least a water monolayer covering their surface in order to become biologically active. We study how the properties of water and the effect of its coupling with the hydrophilic moieties of proteins govern the regime of protein activity. In particular we follow, by means of Fourier Transform Infrared spectroscopy, the thermal evolution of the amide vibrational modes of hydrated lysozyme in the temperature interval 180 K < T < 350 K. In such a way we are able to observe the thermal limit of biological activity characterizing hydrated lysozyme. Finally we focus on the region of lysozyme thermal denaturation by following the evolution of the proton Nuclear Magnetic Resonance (NMR) spectra for 298 K < T < 366 K with the High-Resolution Magic Angle Spinning probe. Our data suggest that the hydrogen bond coupling between hydration water and protein hydrophilic groups is crucial in triggering the main mechanisms that define the enzymatic activity of proteins.
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