We have located links that may give you full text access.
Low-Temperature Decoupling of Water and Protein Dynamics Measured by Neutron Scattering.
Journal of Physical Chemistry Letters 2017 October 6
Water plays a major role in biosystems, greatly contributing to determine their structure, stability, and function. It is well known, for instance, that proteins require a minimum amount of water to be fully functional. Despite many years of intensive research, however, the detailed nature of protein-hydration water interactions is still partly unknown. The widely accepted "protein dynamical transition" scenario is based on perfect coupling between the dynamics of proteins and that of their hydration water, which has never been probed in depth experimentally. I present here high-resolution elastic neutron scattering measurements of the atomistic dynamics of lysozyme in water. The results show for the first time that the dynamics of proteins and of their hydration water are actually decoupled at low temperatures. This important result challenges the "protein dynamical transition" scenario and requires a new model to link protein dynamics to the dynamics of its hydration water.
Full text links
Related Resources
Trending Papers
Heart failure with preserved ejection fraction: diagnosis, risk assessment, and treatment.Clinical Research in Cardiology : Official Journal of the German Cardiac Society 2024 April 12
Proximal versus distal diuretics in congestive heart failure.Nephrology, Dialysis, Transplantation 2024 Februrary 30
Efficacy and safety of pharmacotherapy in chronic insomnia: A review of clinical guidelines and case reports.Mental Health Clinician 2023 October
World Health Organization and International Consensus Classification of eosinophilic disorders: 2024 update on diagnosis, risk stratification, and management.American Journal of Hematology 2024 March 30
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app
All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.
By using this service, you agree to our terms of use and privacy policy.
Your Privacy Choices
You can now claim free CME credits for this literature searchClaim now
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app