Chu, Xiang-qiang Faraone, Antonio Kim, Chansoo Fratini, Emiliano Baglioni, Piero Leao, Juscelino B. Chen, Sow-Hsin 2024-01-20T21:33:13Z 2024-01-20T21:33:13Z 2021-09-03 2009-04-16 1520-6106 https://pubs.kist.re.kr/handle/201004/132565 The low-temperature behavior of proteins under high pressure is not as extensively investigated as that at ambient pressure. In this paper, we study the dynamics of a hydrated protein under moderately high pressures at low temperatures using the quasielastic neutron scattering method. We show that when applying pressure to the protein-water system, the dynamics of the protein hydration water does not slow down but becomes faster instead. The degree of "softness" of the protein, which is intimately related to the enzymatic activity of the protein, shows the same trend as its hydration water as a function of temperature at different pressures. These two results taken together suggest that at lower temperatures, the protein remains soft and active under pressure. English AMER CHEMICAL SOC DYNAMICAL TRANSITION NEUTRON-SCATTERING HYDRATION-WATER LIQUID-PHASE BIOCHEMISTRY CROSSOVER LYSOZYME Proteins Remain Soft at Lower Temperatures under Pressure Article 10.1021/jp900557w 1 JOURNAL OF PHYSICAL CHEMISTRY B, v.113, no.15, pp.5001 - 5006 JOURNAL OF PHYSICAL CHEMISTRY B 113 15 5001 5006 scie scopus 000265030500005 2-s2.0-65249095532 Chemistry, Physical Chemistry Article DYNAMICAL TRANSITION NEUTRON-SCATTERING HYDRATION-WATER LIQUID-PHASE BIOCHEMISTRY CROSSOVER LYSOZYME