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Title: Extended conformations of bifurcating electron transfer flavoprotein constitute up to half the population, possibly mediating conformational change

Journal Article · · Chemical Science
DOI: https://doi.org/10.1039/D4SC04544K · OSTI ID:2478047
ORCiD logo [1];  [2];  [2];  [3];  [4]; ORCiD logo [4];  [2]; ORCiD logo [5]
  1. Department of Chemistry, University of Kentucky, Lexington, KY 40506, USA, Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA
  2. Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA
  3. National Synchrotron Light Source II, Brookhaven National Laboratory, Upton, NY 11973, USA
  4. Department of Chemistry, Technische Universität Berlin, 10623 Berlin, Germany
  5. Department of Chemistry, University of Kentucky, Lexington, KY 40506, USA

Small-angle neutron scattering shows that electron transfer flavoprotein in solution populates extended conformations that are distinct from crystal structures. Extended conformations could mediate conformation changes that gate electron transfer.

Sponsoring Organization:
USDOE
Grant/Contract Number:
NONE; SC0021283; SC0012704
OSTI ID:
2478047
Journal Information:
Chemical Science, Journal Name: Chemical Science Journal Issue: 45 Vol. 15; ISSN 2041-6520; ISSN CSHCBM
Publisher:
Royal Society of Chemistry (RSC)Copyright Statement
Country of Publication:
United Kingdom
Language:
English

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