Water Thermodynamics and Its Effects on the Protein Stability and Activity
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biophysica-01-00030.pdf
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792.9 KB
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Checksum (MD5)
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Author(s)
Mallamace, Francesco
Mallamace, Domenico
Chen, Sow-Hsin
Lanzafame, Paola
Papanikolaou, Georgia
Date Issued
October 2021
Journal
Biophysica
Publisher
Multidisciplinary Digital Publishing Institute
Citation
Biophysica 1 (4): 413-428 (2021)
Version
Final published version
Abstract
We discuss a phenomenon regarding water that was until recently a subject of scientific interest: i.e., the dynamical crossover, from the fragile to strong glass forming material, for both bulk and protein hydration water. Such crossover is characterized by a temperature TL in which significant dynamical changes like the decoupling (or the violation of the Stokes-Einstein relation) of homologous transport parameters, e.g., the density relaxation time τ and the viscosity η, occur in the system. On this respect we considered the dynamic properties of water-protein systems. More precisely, we focused our study on proteins and their hydration water, as far as bulk and confined water. In order to clarify the effects of the water dynamical crossover on the protein properties we considered and discussed in a comparative way previous and new experimental data, obtained from different techniques and molecular dynamic simulation (MD). We pointed out the reasons for different dynamical findings from the use of different experimental techniques.
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/biophysica1040030
