Dynamics of Apolipoprotein B-100 in Interaction with Detergent Probed by Incoherent Neutron Scattering

Cisse, Aline; Schachner-Nedherer, Anna-Laurence; Appel, Markus; Beck, Christian; Ollivier, Jacques; Leitinger, Gerd; Ruth, Peter; Kornmueller, Karin; Peters, Judith

doi:10.1021/acs.jpclett.1c03141

Cited by 12 publications

(11 citation statements)

References 61 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Since the signal is typically dominated by incoherent scattering, the q-dependence mainly influences the different dynamic features. While this approach includes the separation of the (apparent) global diffusion from internal diffusive processes [8], the same procedure can be applied to separate the scattering signal of the crowders from the one of the protein of interest [23], the contributions of monomers and crystals [30], the contributions of two different proteins [31], or to distinguish the scattering signal of proteins from the one coming from the detergent used for purification [32].…”

Section: Discussionmentioning

confidence: 99%

Notes on Fitting and Analysis Frameworks for QENS Spectra of (Soft) Colloid Suspensions

et al. 2022

Self Cite

View full text Add to dashboard Cite

With continuously improving signal-to-noise ratios, a statistically sound analysis of quasi-elastic neutron scattering (QENS) spectra requires to fit increasingly complex models which poses several challenges. Simultaneous fits of the spectra for all recorded values of the momentum transfer become a standard approach. Spectrometers at spallation sources can have a complicated non-Gaussian resolution function which has to be described most accurately. At the same time, to speed up the fitting, an analytical convolution with this resolution function is of interest. Here, we discuss basic concepts to efficient approaches for fits of QENS spectra based on standard MATLAB and Python fit algorithms. We illustrate the fits with example data from IN16B, BASIS, and BATS.

show abstract

Section: Discussionmentioning

confidence: 99%

Notes on Fitting and Analysis Frameworks for QENS Spectra of (Soft) Colloid Suspensions

et al. 2022

Self Cite

View full text Add to dashboard Cite

show abstract

“…In relation to this study on LDL, the characterization of apo B-100 has recently been conducted using QENS [ 75 ]. Since apo B-100 is an amphiphilic protein, the use of detergents called Nonidet P-40 (NP40) was necessary to solubilize the protein.…”

Section: Ins Studies On Pathologically Relevant Bio-macromoleculesmentioning

confidence: 99%

Sub-Nanosecond Dynamics of Pathologically Relevant Bio-Macromolecules Observed by Incoherent Neutron Scattering

Matsuo

Peters

2022

Life

Self Cite

View full text Add to dashboard Cite

Incoherent neutron scattering (iNS) is one of the most powerful techniques to study the dynamical behavior of bio-macromolecules such as proteins and lipid molecules or whole cells. This technique has widely been used to elucidate the fundamental aspects of molecular motions that manifest in the bio-macromolecules in relation to their intrinsic molecular properties and biological functions. Furthermore, in the last decade, iNS studies focusing on a possible relationship between molecular dynamics and biological malfunctions, i.e., human diseases and disorders, have gained importance. In this review, we summarize recent iNS studies on pathologically relevant proteins and lipids and discuss how the findings are of importance to elucidate the molecular mechanisms of human diseases and disorders that each study targets. Since some diseases such as amyloidosis have become more relevant in the aging society, research in this field will continue to develop further and be more important in the current increasing trend for longevity worldwide.

show abstract

“…Up to now, the separation of different diffusive contributions was possible either due to partial deuteration of the samples investigated 39 or to the use of advanced modeling in hydrated powders. 41 Here, we test the predicted bulk behavior of an aqueous solution of two distinct tracer proteins, namely, bovine serum albumin (BSA) and bovine polyclonal gamma-globulin (Ig). We separate the apparent center-of-mass diffusion coefficients measured simultaneously for both proteins from the internal diffusive processes and the solvent contributions.…”

Section: Introductionmentioning

confidence: 99%

“…Hence, a dedicated study of a model polydisperse system with tunable tracer composition is necessary, which in its simplest case would be a bidisperse system with a tunable total volume fraction and relative composition. Up to now, the separation of different diffusive contributions was possible either due to partial deuteration of the samples investigated or to the use of advanced modeling in hydrated powders . Here, we test the predicted bulk behavior of an aqueous solution of two distinct tracer proteins, namely, bovine serum albumin (BSA) and bovine polyclonal gamma-globulin (Ig).…”

Section: Introductionmentioning

confidence: 99%

Short-Time Transport Properties of Bidisperse Suspensions of Immunoglobulins and Serum Albumins Consistent with a Colloid Physics Picture

Beck

Grimaldo²,

López

et al. 2022

J. Phys. Chem. B

Self Cite

View full text Add to dashboard Cite

The crowded environment of biological systems such as the interior of living cells is occupied by macromolecules with a broad size distribution. This situation of polydispersity might influence the dependence of the diffusive dynamics of a given tracer macromolecule in a monodisperse solution on its hydrodynamic size and on the volume fraction. The resulting size dependence of diffusive transport crucially influences the function of a living cell. Here, we investigate a simplified model system consisting of two constituents in aqueous solution, namely, of the proteins bovine serum albumin (BSA) and bovine polyclonal gamma-globulin (Ig), systematically depending on the total volume fraction and ratio of these constituents. From high-resolution quasi-elastic neutron spectroscopy, the separate apparent short-time diffusion coefficients for BSA and Ig in the mixture are extracted, which show substantial deviations from the diffusion coefficients measured in monodisperse solutions at the same total volume fraction. These deviations can be modeled quantitatively using results from the short-time rotational and translational diffusion in a two-component hard sphere system with two distinct, effective hydrodynamic radii. Thus, we find that a simple colloid picture well describes short-time diffusion in binary mixtures as a function of the mixing ratio and the total volume fraction. Notably, the self-diffusion of the smaller protein BSA in the mixture is faster than the diffusion in a pure BSA solution, whereas the self-diffusion of Ig in the mixture is slower than in the pure Ig solution.

show abstract

Dynamics of Apolipoprotein B-100 in Interaction with Detergent Probed by Incoherent Neutron Scattering

Cited by 12 publications

References 61 publications

Notes on Fitting and Analysis Frameworks for QENS Spectra of (Soft) Colloid Suspensions

Notes on Fitting and Analysis Frameworks for QENS Spectra of (Soft) Colloid Suspensions

Sub-Nanosecond Dynamics of Pathologically Relevant Bio-Macromolecules Observed by Incoherent Neutron Scattering

Short-Time Transport Properties of Bidisperse Suspensions of Immunoglobulins and Serum Albumins Consistent with a Colloid Physics Picture

Contact Info

Product

Resources

About