Proton Zero Point Energy Effects on the Folding of Proteins

DOI

Earlier experiment at ISIS have shown that water responds to the distortion of the hydrogen bond network by delocalizing some of the protons in the vicinity of the defects. That these quantum effects are significant for the folding or unfolding of the protein molecules has been shown by the experiment for which this proposal is a continuation. We examined the momentum distribution for the protons in a dilute solution of lysozyme in water, as the temperature changed through its unfolding transition, 300-340K, and found the expected increase and subsequent decrease of the kinetic energy. That experiment showed that the effect on the water of the unfolding of the protein is not limited to the surface of the protein. We wish to repeat the experiment at a higher concentrations of protein to both confirm the initial experiment and estimate the range of influence of the protein.

Identifier
DOI https://doi.org/10.5286/ISIS.E.24079796
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/24079796
Provenance
Creator Professor George Reiter; Professor Roberto Senesi
Publisher ISIS Neutron and Muon Source
Publication Year 2013
Rights CC-BY Attribution 4.0 International; https://creativecommons.org/licenses/by/4.0/
OpenAccess true
Contact isisdata(at)stfc.ac.uk
Representation
Resource Type Dataset
Discipline Photon- and Neutron Geosciences
Temporal Coverage Begin 2010-05-21T08:07:34Z
Temporal Coverage End 2010-07-10T07:11:33Z