Mechanism of Trehalose-Induced Protein Stabilization from Neutron Scattering and Modeling

2019 ◽  
Vol 123 (17) ◽  
pp. 3679-3687 ◽  
Author(s):  
Christoffer Olsson ◽  
Samuel Genheden ◽  
Victoria García Sakai ◽  
Jan Swenson
Keyword(s):  
Neutron Scattering ◽  
Protein Stabilization

scholarly journals Confinement Facilitated Protein Stabilization As Investigated by Small-Angle Neutron Scattering

2018 ◽  
Vol 140 (40) ◽  
pp. 12720-12723 ◽  
Author(s):  
Justin Siefker ◽  
Ralf Biehl ◽  
Margarita Kruteva ◽  
Artem Feoktystov ◽  
Marc-Olivier Coppens
Keyword(s):  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Protein Stabilization

scholarly journals Direct localization of detergents and bacteriorhodopsin in the lipidic cubic phase by small-angle neutron scattering

IUCrJ ◽  
2021 ◽  
Vol 8 (1) ◽  
pp. 22-32
Author(s):  
Thomas Cleveland IV ◽  
Emily Blick ◽  
Susan Krueger ◽  
Anna Leung ◽  
Tamim Darwish ◽  
...  
Keyword(s):  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Selection Process ◽  
Protein Stabilization ◽  
Cubic Phase ◽  
Octyl Glucoside ◽  
Lipidic Cubic Phase ◽  
Contrast Matching ◽  
And Behavior

Lipidic cubic phase (LCP) crystallization methods have been essential in obtaining crystals of certain membrane proteins, particularly G-protein-coupled receptors. LCP crystallization is generally optimized across a large number of potential variables, one of which may be the choice of the solubilizing detergent. A better fundamental understanding of the behavior of detergents in the LCP may guide and simplify the detergent selection process. This work investigates the distribution of protein and detergent in LCP using the membrane protein bacteriorhodopsin (bR), with the LCP prepared from highly deuterated monoolein to allow contrast-matched small-angle neutron scattering. Contrast-matching allows the scattering from the LCP bilayer itself to be suppressed, so that the distribution and behavior of the protein and detergent can be directly studied. The results showed that, for several common detergents, the detergent micelle dissociates and incorporates into the LCP bilayer essentially as free detergent monomers. In addition, the detergent octyl glucoside dissociates from bR, and neither the protein nor detergent forms clusters in the LCP. The lack of detergent assemblies in the LCP implies that, upon incorporation, micelle sizes and protein/detergent interactions become less important than they would be in solution crystallization. Crystallization screening confirmed this idea, with crystals obtained from bR in the presence of most detergents tested. Thus, in LCP crystallization, detergents can be selected primarily on the basis of protein stabilization in solution, with crystallization suitability a lesser consideration.

Local atomic structure of relaxor ferroelectric solids studied by pulsed neutron scattering

1994 ◽  
Vol 52 ◽  
pp. 554-555
Author(s):  
T. Egami ◽  
H. D. Rosenfeld ◽  
S. Teslic
Keyword(s):  
Neutron Scattering ◽  
Atomic Structure ◽  
Argonne National Laboratory ◽  
Relaxor Ferroelectrics ◽  
Relaxor Ferroelectric ◽  
Crystallographic Structure ◽  
Chemical Inhomogeneity ◽  
Distribution Analysis ◽  
Ferroelectric Transition ◽  
Pulsed Neutron

Relaxor ferroelectrics, such as Pb(Mg1/3Nb2/3)O3 (PMN) or (Pb·88La ·12)(Zr·65Ti·35)O3 (PLZT), show diffuse ferroelectric transition which depends upon frequency of the a.c. field. In spite of their wide use in various applications details of their atomic structure and the mechanism of relaxor ferroelectric transition are not sufficiently understood. While their crystallographic structure is cubic perovskite, ABO3, their thermal factors (apparent amplitude of thermal vibration) is quite large, suggesting local displacive disorder due to heterovalent ion mixing. Electron microscopy suggests nano-scale structural as well as chemical inhomogeneity.We have studied the atomic structure of these solids by pulsed neutron scattering using the atomic pair-distribution analysis. The measurements were made at the Intense Pulsed Neutron Source (IPNS) of Argonne National Laboratory. Pulsed neutrons are produced by a pulsed proton beam accelerated to 750 MeV hitting a uranium target at a rate of 30 Hz. Even after moderation by a liquid methane moderator high flux of epithermal neutrons with energies ranging up to few eV’s remain.

Sign in / Sign up

Export Citation Format

Share Document