The spin-echo spectrometer at the Spallation Neutron Source (SNS)

Ohl, Michael; Monkenbusch, M.; Arend, N.; Kozielewski, T.; Vehres, G.; Tiemann, C.; Butzek, Michael; Soltner, H.; Giesen, U.; Achten, R.; Stelzer, H.; Lindenau, B.; Budwig, A.; Kleines, H.; Drochner, M.; P.Kaemmerling,; Wagener, Michael; Moeller, R.; Iverson, Erik B.; Sharp, Melissa; Richter, D.

doi:10.1016/j.nima.2012.08.059

Cited by 89 publications

(71 citation statements)

References 21 publications

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“…The NSE experiment was performed at SNS-NSE instrument, JCNS1 outstation to Spallation Neutron Source, Oak Ridge National Laboratory [67]. NSE spectra were measured at a maximum incident wavelength of 9Å, accessing a dynamical range of ≤0.1 t max ≤70 ns (Fouriertimes) for several momentum transfers, Q, between 0.05Å −1 and 0.12Å −1 .…”

Section: Methodsmentioning

confidence: 99%

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Controllable Activation of Nanoscale Dynamics in a Disordered Protein Alters Binding Kinetics

Callaway

Matsui

Weiß

et al. 2017

Journal of Molecular Biology

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Phosphorylation of S339/S340 in the disordered tail of the multi-domain scaffolding protein NHERF1 affects the intracellular localization and trafficking of NHERF1 assembled signaling complexes. Using neutron spin echo spectroscopy (NSE), we show salt concentration dependent excitation of nanoscale motion at the tip of the C-terminal tail in the phosphomimic S339D/S340D mutant. The “tip of the whip” that is unleashed is near the S339/S340 phosphorylation site and flanks the hydrophobic Ezrin-binding motif. Further, we show that the kinetic association rate constant of the binding of the S339D/S340D mutant to the FERM domain of Ezrin is sensitive to buffer salt concentration, correlating with the excited nanoscale dynamics. The results demonstrate that nanoscale dynamics of an intrinsically disordered protein influences the binding kinetics of signaling partners. NSE can pinpoint the nanoscale dynamics changes in a highly specific manner.

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Section: Methodsmentioning

confidence: 99%

“…Solvent/background measurement and transmission measurements were also necessary for proper data reduction. The data reduction was performed with the standard ECHODET software package of the NSE-SNS instrument [67]. The momentum transfer (Q) ranges between 0.052 and 0.169 Å −1 .…”

Section: Methodsmentioning

confidence: 99%

Controllable Activation of Nanoscale Dynamics in a Disordered Protein Alters Binding Kinetics

Callaway

Matsui

Weiß

et al. 2017

Journal of Molecular Biology

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“…It is therefore an ideal tool to probe the bilayer's undulational motions, which are characteristic of bending rigidity 23 . We performed NSE measurements 24 NSE measurements report the intermediate scattering function (ISF), or S(q,τ)/S(q,0). This can be thought of as the probability of finding atomic pair correlations at a distance, 2π/q, after a time, τ (Figs.…”

Section: Determination Of Nanodomain Bending Modulusmentioning

confidence: 99%

Mechanical Properties of Nanoscopic Lipid Domains

et al. 2015

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The lipid raft hypothesis presents insights into how the cell membrane organizes proteins and lipids to accomplish its many vital functions. Yet basic questions remain about the physical mechanisms that lead to the formation, stability, and size of lipid rafts. As a result, much interest has been generated in the study of systems that contain similar lateral heterogeneities, or domains. In the current work we present an experimental approach that is capable of isolating the bending moduli of lipid domains. This is accomplished using neutron scattering and its unique sensitivity to the isotopes of hydrogen. Combining contrast matching approaches with inelastic neutron scattering, we isolate the bending modulus of ∼13 nm diameter domains residing in 60 nm unilamellar vesicles, whose lipid composition mimics the mammalian plasma membrane outer leaflet. Importantly, the bending modulus of the nanoscopic domains differs from the modulus of the continuous phase surrounding them. From additional structural measurements and all-atom simulations, we also determine that nanoscopic domains are in-register across the bilayer leaflets. Taken together, these results inform a number of theoretical models of domain/raft formation and highlight the fact that mismatches in bending modulus must be accounted for when explaining the emergence of lateral heterogeneities in lipid systems and biological membranes.

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“…The measurements were done at the SNS-NSE spectrometer at SNS [5,6], modified to have a setup shown in Fig. 3.…”

Section: Methodsmentioning

confidence: 99%

Quasielastic neutron scattering experiment on water using TOFLAR (Time Of Flight and LARmor precession) technique at SNS

Kusmin

Eijck

Pappas

et al. 2015

EPJ Web of Conferences

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Abstract. We present the results of the first TOFLAR (Time Of Flight and LARmor precession) experiment with a Larmor modulation device positioned after the sample. Using a setup based on the configuration of the SNS-NSE spectrometer (Spallation Neutron Source, USA), we did TOFLAR measurements on water at 5 and 20 degree Celsius, analyzed the spectra, and obtained diffusion coefficient values that are in a reasonable agreement with literature. Thus, our results demonstrate that TOFLAR may become a standard technique to study quasielastic neutron scattering in future.

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The spin-echo spectrometer at the Spallation Neutron Source (SNS)

Cited by 89 publications

References 21 publications

Controllable Activation of Nanoscale Dynamics in a Disordered Protein Alters Binding Kinetics

Controllable Activation of Nanoscale Dynamics in a Disordered Protein Alters Binding Kinetics

Mechanical Properties of Nanoscopic Lipid Domains

Quasielastic neutron scattering experiment on water using TOFLAR (Time Of Flight and LARmor precession) technique at SNS

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