Transition and signature of protein domain motion in Phosphoglyceratekinase (PGK) into the regime of local modes

DOI

In a series of neutron spin-echo experiments (NSE) on the proteins alcohol dehydrogenase (ADH) and phosphoglycerate kinase (PGK) large scale large amplitude domain motions with functional relevance have been observed. Our NSE experiments covered momentum transfer values up to 0.2Å-1. For larger Q-value the mixture of coherent and incoherent signal contributions with amplitude factors 1 and -1/3 respectively makes the NSE experiment tedious. The extension of the accessed Q range by the here proposed TOF experiment on PGK will explore how the inferred model extends from the low Q into the high(er)-Q behavior, relating large scale domain motions to more local fluctuations observed by TOF.

Identifier
DOI https://doi.org/10.5286/ISIS.E.24090597
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/24090597
Provenance
Creator Dr Andreas Stadler; Dr Ralf Biehl; Dr Michael Monkenbusch
Publisher ISIS Neutron and Muon Source
Publication Year 2016
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 2013-05-20T11:23:04Z
Temporal Coverage End 2013-05-29T08:08:09Z