2008/10/07 by Xiang-qiang Chu, Antonio Faraone, Chu, Xiang-qiang +11
Biochemistry, Genetics and Molecular Biology · Chemistry · Materials Science · #Biological Physics (physics.bio-ph) #Enzyme Structure and Function #FOS: Physical sciences #Protein Structure and Dynamics #thermodynamics and calorimetric analyses
paper · pdf · doi:10.48550/arxiv.0810.1228
openalex publication_date 2008/10/07 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
Recently we have shown experimental evidence for a fragile-to-strong dynamic crossover (FSC) phenomenon in hydration water around a globular protein (lysozyme) at ambient pressure. In this letter we show that when applying pressure to the protein-water system, the FSC crossover temperatures in hydration water of lysozyme tracks the similar Widom line emanating from the existence of a liquid-liquid critical point in a 1-D confined water (in MCM-41-S). The mean squared displacements (MSD) of hydrogen atoms in lysozyme and in its hydration water show a sudden change of slopes at the same characteristic temperature, which decreases with an increasing pressure. These results taken together give support of the idea that the dynamic crossover (or so-called glass transition) of the protein is a function of both temperature and pressure, following the FSC of its hydration water.