Dynamics of lysozyme and its hydration water under electric field
Abstract
The effects of static electric field on the dynamics of lysozyme and its hydration water have been investigated by means of incoherent quasi-elastic neutron scattering (QENS). Measurements were performed on lysozyme samples, hydrated respectively with heavy water (D2O) to capture the protein dynamics, and with light water (H2O), to probe the dynamics of the hydration shell, in the temperature range from 210 < T < 260 K. The hydration fraction in both cases was about 0.38 gram of water per gram of dry protein. The field strengths investigated were respectively 0 kV/mm and 2 kV/mm ( 2 106 V/m) for the protein hydrated with D2O and 0 kV and 1 kV/mm for the H2O-hydrated counterpart. While the overall internal protons dynamics of the protein appears to be unaffected by the application of electric field up to 2 kV/mm, likely due to the stronger intra-molecular interactions, there is also no appreciable quantitative enhancement of the diffusive dynamics of the hydration water, as would be anticipated based on our recent observations in water confined in silica pores under field values of 2.5 kV/mm. This may be due to the difference in surface interactions between water and the two adsorption hosts (silica andmore »
- Authors:
-
- ORNL
- North Carolina State University
- Publication Date:
- Research Org.:
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Center for Structural Molecular Biology (CSMB)
- Sponsoring Org.:
- USDOE Office of Science (SC)
- OSTI Identifier:
- 1149393
- DOE Contract Number:
- DE-AC05-00OR22725
- Resource Type:
- Journal Article
- Journal Name:
- Journal of Biological Physics
- Additional Journal Information:
- Journal Volume: 40; Journal Issue: 2; Journal ID: ISSN 0092--0606
- Country of Publication:
- United States
- Language:
- English
- Subject:
- Electric Field; Protein Dynamics; DIffusion; Quasi-Elastic Neutron Scatteirng
Citation Formats
Favi, Pelagie M, Zhang, Qiu, O'Neill, Hugh Michael, Mamontov, Eugene, Omar Diallo, Souleymane, and Palmer, Jeremy. Dynamics of lysozyme and its hydration water under electric field. United States: N. p., 2014.
Web. doi:10.1007/s10867-014-9343-2.
Favi, Pelagie M, Zhang, Qiu, O'Neill, Hugh Michael, Mamontov, Eugene, Omar Diallo, Souleymane, & Palmer, Jeremy. Dynamics of lysozyme and its hydration water under electric field. United States. https://doi.org/10.1007/s10867-014-9343-2
Favi, Pelagie M, Zhang, Qiu, O'Neill, Hugh Michael, Mamontov, Eugene, Omar Diallo, Souleymane, and Palmer, Jeremy. 2014.
"Dynamics of lysozyme and its hydration water under electric field". United States. https://doi.org/10.1007/s10867-014-9343-2.
@article{osti_1149393,
title = {Dynamics of lysozyme and its hydration water under electric field},
author = {Favi, Pelagie M and Zhang, Qiu and O'Neill, Hugh Michael and Mamontov, Eugene and Omar Diallo, Souleymane and Palmer, Jeremy},
abstractNote = {The effects of static electric field on the dynamics of lysozyme and its hydration water have been investigated by means of incoherent quasi-elastic neutron scattering (QENS). Measurements were performed on lysozyme samples, hydrated respectively with heavy water (D2O) to capture the protein dynamics, and with light water (H2O), to probe the dynamics of the hydration shell, in the temperature range from 210 < T < 260 K. The hydration fraction in both cases was about 0.38 gram of water per gram of dry protein. The field strengths investigated were respectively 0 kV/mm and 2 kV/mm ( 2 106 V/m) for the protein hydrated with D2O and 0 kV and 1 kV/mm for the H2O-hydrated counterpart. While the overall internal protons dynamics of the protein appears to be unaffected by the application of electric field up to 2 kV/mm, likely due to the stronger intra-molecular interactions, there is also no appreciable quantitative enhancement of the diffusive dynamics of the hydration water, as would be anticipated based on our recent observations in water confined in silica pores under field values of 2.5 kV/mm. This may be due to the difference in surface interactions between water and the two adsorption hosts (silica and protein), or to the existence of a critical threshold field value Ec 2 3 kV/mm for increased molecular diffusion, for which electrical breakdown is a limitation for our sample.},
doi = {10.1007/s10867-014-9343-2},
url = {https://www.osti.gov/biblio/1149393},
journal = {Journal of Biological Physics},
issn = {0092--0606},
number = 2,
volume = 40,
place = {United States},
year = {Wed Jan 01 00:00:00 EST 2014},
month = {Wed Jan 01 00:00:00 EST 2014}
}