Protein dynamics by neutron scattering: The protein dynamical transition and the fragile-to-strong dynamical crossover in hydrated lysozyme

被引：6
|
作者：
Magazu, Salvatore [1 ]
Migliardo, Federica [1 ]
Benedetto, Antonio [2 ,3 ]
Vertessy, Beata [4 ]
机构：
[1] Univ Messina, Dipartimento Fis, I-98166 Messina, Italy
[2] Univ Coll Dublin, Sch Phys, Dublin 2, Ireland
[3] Univ Sydney, Sydney Med Sch, Sch Med Sci, Sydney, NSW 2006, Australia
[4] Hungarian Acad Sci, Inst Enzymol, H-1113 Budapest, Hungary
来源：
CHEMICAL PHYSICS | 2013年 / 424卷
关键词：
Dynamical transition; Mean square displacement; Lysozyme; Bioprotectant; Resolution effects; Vibrational motion amplitude; Elastic neutron scattering; MEAN-SQUARE DISPLACEMENT; GLASS-TRANSITION; ENZYME-ACTIVITY; WATER; RESOLUTION; PUZZLE;
D O I：
10.1016/j.chemphys.2013.03.001
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
In this work Elastic Incoherent Neutron Scattering (EINS) results on lysozyme water mixtures in absence and in presence of bioprotectant systems are presented. The EINS data have been collected by using the IN13 and the IN10 spectrometers at the Institut Laue-Langevin (ILL, Grenoble, France) allowing to evaluate the temperature behaviour of the mean square displacement and of the relaxation time for the investigated systems. The obtained experimental findings together with theoretical calculations allow to put into evidence the role played by the spectrometer resolution and to clarify the connexion between the registered protein dynamical transition, the system relaxation time, and the instrumental energy resolution. (C) 2013 Elsevier B. V. All rights reserved.
引用
收藏
页码：26 / 31
页数：6
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