| 1. |
- Nylander, Tommy, et al.
(författare)
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Relationship between Structure and Fluctuations of Lipid Nonlamellar Phases Deposited at the Solid-Liquid Interface
- 2017
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Ingår i: Journal of Physical Chemistry B. - : American Chemical Society (ACS). - 1520-6106 .- 1520-5207. ; 121:13, s. 2705-2711
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Tidskriftsartikel (refereegranskat)abstract
- The structure and dynamics of nanostructure films formed by mixtures of soy phosphatidylcholine and glycerol dioleate at the silicon aqueous interface were studied by grazing incidence neutron spin echo spectroscopy (GINSES), specular and off-specular neutron, reflectometry, and small-angle X-ray diffraction. Reverse hexagonal (Hr) and micellar cubic phase (Fd3m) layers at: the solid liquid interface have been identified with neutron reflectometry measurements. A preferred orientation of the liquid crystalline (LC) domains was observed only for the anisotropic,H-II phase. The size of the LC domains was found to be about 1 micrometer as estimated from the width of the diffraction peaks. GINSES revealed that the cubic phase forms rather rigid films. In comparison, the HE film was more flexible, appearing as a modified undulation spectrum of the cylinders due to the interaction with the substrate.
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| 2. |
- Bucciarelli, Saskia, et al.
(författare)
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Dramatic influence of patchy attractions on short-time protein diffusion under crowded conditions
- 2016
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Ingår i: Science Advances. - : American Association for the Advancement of Science (AAAS). - 2375-2548. ; 2:12, s. 1601432-1601432
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Tidskriftsartikel (refereegranskat)abstract
- In the dense and crowded environment of the cell cytoplasm, an individual protein feels the presence of and interacts with all surrounding proteins. While we expect this to strongly influence the short-time diffusion coefficient Ds of proteins on length scales comparable to the nearest-neighbor distance, this quantity is difficult to assess experimentally. We demonstrate that quantitative information about Ds can be obtained from quasi-elastic neutron scattering experiments using the neutron spin echo technique. We choose two well-characterized and highly stable eye lens proteins, bovine α-crystallin and γB-crystallin, and measure their diffusion at concentrations comparable to those present in the eye lens. While diffusion slows down with increasing concentration for both proteins, we find marked variations that are directly linked to subtle differences in their interaction potentials. A comparison with computer simulations shows that anisotropic and patchy interactions play an essential role in determining the local short-time dynamics. Hence, our study clearly demonstrates the enormous effect that weak attractions can have on the short-time diffusion of proteins at concentrations comparable to those in the cellular cytosol.
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