Water and lysozyme： Some results from the bending and stretching vibrational modes

作     者：FrancescoMallamace Carmelo Corsaro Domenico Mallamace Cirino Vasi Nicola Cicero H. Eugene Stanley 

作者机构：Dipartimento di Fisica e Scienze della Terra Universita di Messina 1-98166 Messina Italy Department of Nuclear Science and Engineering Massachusetts Institute of Technology Cambridge MA 02139 USA Center for Polymer Studies and Department of Physics Boston University Boston MA 02215 USA Consiglio Nazionale delle Ricerche-IPCF Messina 1-98166 Messina Italy Dipartimento di Scienze dell'Ambiente della Sicurezza del Territorio degli Alimenti e della Salute Universita di Messina Viale F. Stagno d'Alcontres 31 98166 Messina Italy 

出 版 物：《Frontiers of physics》 (物理学前沿（英文版）)

年 卷 期：2015年第10卷第5期

页      面：27-34页

核心收录：

学科分类：07[理学] 08[工学] 070203[理学-原子与分子物理] 0827[工学-核科学与技术] 082701[工学-核能科学与工程] 0704[理学-天文学] 0702[理学-物理学] 

主　　题：protein unfolding hydration water infrared spectroscopy 

摘      要：The dynamic or glass transition in biomolecules is important to their functioning. Also essential is the transition between the protein native state and the unfolding process. To better understand these transitions, we use Fourier transform infrared spectroscopy to study the vibrational bending and stretching modes of hydrated lysozymes across a wide temperature range. We find that these transitions are triggered by the strong hydrogen bond coupling between the protein and hydration water. More precisely, we demonstrate that in both cases the water properties dominate the evolution of the system. We find that two characteristic temperatures are relevant： in the supercooled regime of confined water, the fragile-to-strong dynamic transition occurs at TL, and in the stable liquid phase, T＊ 315 ± 5 K characterizes the behavior of both isothermal compressibility KT（T, P） and the coefficient of thermal expansion ap（T, P）.