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At least 181 records · Page 10Linked to original sources
PubMed1994

MgATP-induced conformational changes in the iron protein from Azotobacter vinelandii, as studied by small-angle x-ray scattering.

Small angle x-ray scattering experiments have been carried out on the purified iron proteins of nitrogenase from wild-type Azotobacter vinelandii and from a Nif- mutant strain, A. vinelandii UW91 (which has an A157S mutation). This study was designed to investigate the influence of MgATP and MgADP binding on the protein structure in solution. For the wild-type protein, the binding of MgATP induces a significant conformational change that is observed as a decrease of about 2.0 A in the radius of gyration. In contrast, the binding of MgADP to the wild-type iron protein does not detectably affect the radius of gyration. In the absence of nucleotides, the radius of gyration for the UW91 mutant is indistinguishable from that of the wild-type. However, unlike for the wild-type protein, the radius of gyration of the UW91 iron protein is unaffected by the addition of MgATP. We have previously shown that the UW91 iron protein has a normal [4Fe-4S] cluster and MgATP binding ability but that it is completely blocked for electron transfer and MgATP hydrolysis (Gavini, N., and Burgess, B. K. (1992) J. Biol. Chem. 267, 21179-21186). These x-ray scattering measurements suggest that a conformation different from that of the native state is therefore required for the iron protein to perform electron transfer to the MoFe protein. These results also support the hypothesis that Ala-157 is crucial for the iron protein to establish the electron-transfer-favored conformation induced by MgATP binding.

Adenosine Diphosphate↗
PubMed2006

What can we learn about the lipid vesicle structure from the small-angle neutron scattering experiment?

Small-angle neutron scattering (SANS) on the unilamellar vesicle (ULV) populations (diameter 500 and 1,000 A) in D2O was used to characterize lipid vesicles from dimyristoylphosphatidylcholine (DMPC) at three phases: gel Lbeta', ripple Pbeta' and liquid Lalpha. Parameters of vesicle populations and internal structure of the DMPC bilayer were characterized on the basis of the separated form factor (SFF) model. Vesicle shape changes from nearly spherical in the Lalpha phase to elliptical in the Pbeta' and Lbeta' phases. This is true for vesicles prepared via extrusion through pores with the diameter 500 A. Parameters of the internal bilayer structure (thickness of the membrane and the hydrophobic core, hydration and the surface area of the lipid molecule) were determined on the basis of the hydrophobic-hydrophilic (HH) approximation of neutron scattering length density across the bilayer rhox and of the step function (SF) approximation of rhox. DMPC membrane thickness in the Lalpha phase (T = 30 degrees C) demonstrates a dependence on the membrane curvature for extruded vesicles. Prepared via extrusion through 500 A diameter pores, vesicle population in the Lalpha phase has the following characteristics: average value of minor semi-axis 266 +/- 2 A, ellipse eccentricity 1.11 +/- 0.02, polydispersity 26%, thickness of the membrane 48.9 +/- 0.2 A and of the hydrophobic core 19.9 +/- 0.4 A, surface area 60.7 +/- 0.5 A2 and number of water molecules 12.8 +/- 0.3 per DMPC molecule. Vesicles prepared via extrusion through pores with the diameter 1,000 A have polydispersity of 48% and membrane thickness of 45.5 +/- 0.6 A in the Lalpha phase. SF approximation was used to describe the DMPC membrane structure in Lbeta' (T = 10 degrees C) and Pbeta' (T = 20 degrees C) phases. Extruded DMPC vesicles in D2O have membrane thickness of 49.6 +/- 0.5 A in the Lbeta' phase and 48.3 +/- 0.6 A in the Pbeta' phase. The dependence of the DMPC membrane thickness on temperature was restored from the SANS experiment.

Biophysical Phenomena↗
PubMedDate not supplied

An improved electron multiple-scattering distribution for Monte Carlo transport simulation.

An improved electron multiple-scattering distribution is presented in the form of a composite function which combines three expressions valid over different scattering angle regions: a modified relativistic Mott single-scattering term for large angle scattering, a modified Moliere Gaussian term for small angle scattering, and an exponential term for the intermediate angle scattering region. The exponential term has two adjustable parameters which make possible the smooth transition from the large to the small scattering angle regions. The proposed distribution exhibits better agreement with experiment than other multiple-scattering distributions commonly used in Monte Carlo electron transport codes, is amenable to direct sampling over a continuous range of electron energies and step sizes, can be used for elements of any atomic number, and is particularly suitable for use on small memory computers.

Electrons↗
PubMed2006

Static light scattering and small-angle neutron scattering study on aggregated recombinant gelatin in aqueous solution.

Recombinant gelatins are currently evaluated as new excipients for pharmaceutical formulations. They can differ from nonrecombinant gelatins because of intentional alteration of the amino acid sequence and specific properties of the expression systems used. This may affect their solution behavior. In the present work, aqueous solutions of a histidine-containing recombinant gelatin (RG-15-His) were analyzed. Dynamic light scattering (DLS) and loss of absorbance at 200 nm upon centrifugation indicated the formation of aggregates within 1 day upon sample preparation. Static light scattering (SLS) and small-angle neutron scattering (SANS) experiments showed that the aggregate's size was > or =300 nm, and that aggregates are composed of thin, rigid rods of 37 +/- 5 nm in length. The observed aggregation was not detectable by circular dichroism (CD), Fourier transform infrared spectroscopy (FTIR), and cryo transmission electron microscopy (cryo-TEM). SANS experiments, which are not frequently used in the pharmaceutical field, provided additional morphological information about the recombinant gelatin in solution. The results show that combining SLS and SANS is a broadly applicable, complementary approach for detecting aggregation of proteins and other biomolecules and for obtaining structural information about the aggregates.

Gelatin↗
PubMed2001

Bilayer thickness and lipid interface area in unilamellar extruded 1,2-diacylphosphatidylcholine liposomes: a small-angle neutron scattering study.

Small-angle neutron scattering (SANS) experiments have been performed on large unilamellar liposomes prepared from 1,2-dilauroylphosphatidylcholine (DLPC), 1,2-dimyristoyl-phosphatidylcholine (DMPC) and 1,2-distearoylphosphatidylcholine (DSPC) in heavy water by extrusion through polycarbonate filters with 500 A pores. The neutron scattering intensity I(Q) in the region of scattering vectors Q corresponding to 0.0015 A(-2) < or = Q(2) < or = 0.0115 A(-2) was fitted using a step function model of bilayer neutron scattering length density and supposing that the liposomes are spherical and have a Gaussian distribution of radii. Using the lipid volumetric data, and supposing that the thickness of bilayer polar region equals to d(H) = 9+/-1 A and the water molecular volume intercalated in the bilayer polar region is the same as in the aqueous bulk aqueous phase, the steric bilayer thickness d(L), the lipid surface area A(L) and the number of water molecules per lipid molecule N intercalated in the bilayer polar region were obtained: d(L) = 41.58+/-1.93 A, A(L) = 57.18+/-1.00 A(2) and N = 6.53+/-1.93 in DLPC at 20 degrees C, d(L) = 44.26+/-1.42 A, A(L) = 60.01+/-0.75 A(2) and N = 7.37+/-1.94 in DMPC at 36 degrees C, and d(L) = 49.77+/-1.52 A, A(L) = 64.78+/-0.46 A(2) and N = 8.67+/-1.97 in DSPC at 60 degrees C. After correcting for area thermal expansivity alpha approximately 0.00417 K(-1), the lipid surface area shows a decrease with the lipid acyl chain length at 60 degrees C: A(L) = 67.56+/-1.18 A(2) in DLPC, A(L) = 66.33+/-0.83 A(2) in DMPC and A(L) = 64.78+/-0.46 A(2) in DSPC. It is also shown that a joint evaluation of SANS and small-angle X-ray scattering on unilamellar liposomes can be used to obtain the value of d(H) and the distance of the lipid phosphate group from the bilayer hydrocarbon region d(H1).

1,2-Dipalmitoylphosphatidylcholine↗