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1.
Structure of the fully hydrated gel phase of dipalmitoylphosphatidylcholine. 总被引:3,自引:14,他引:3
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X-ray diffraction intensities for lamellar repeats, h = 1 to 7, and wide-angle x-ray scattering were measured for the gel phase of fully hydrated dipalmitoylphosphatidylcholine. A hybrid model, which represents the electron density along the lamellar repeat direction as a continuous function composed of constant strips and superimposed Gaussians, is defined. The data were used to determine the best parameters in hybrid models and also in the older strip models. The most successful results were obtained when the density of the methylene region was constrained to the value obtained from the wide-angle scattering. Further analysis utilized the lipid volume obtained from absolute specific volume measurements. Together with the fundamental relations derived in the previous paper, the electron density modeling yielded the headgroup volume (340 +/- 10 A3) and the methylene volume (25.3 +/- 0.2A3). The results were in agreement whether the hybrid model or the strip model was used and whether our data or the data of Torbet and Wilkins were used. Additional structural results, such as the area (45.9 +/- 2.0 A2) and the number of waters of hydration per lipid (10.6 +/- 2.0), required one additional piece of information, which we took to be the tilt angle theta, which is 30 +/- 3 degrees from other experiments in the literature. Absolute electron density profiles, which clearly indicate two features in the headgroup region, are presented. The analysis yielded an accurate value of F(0), which contributes to the continuous scattering transform F(X), which is also given. 相似文献
2.
The structure of fully hydrated gel phase dimyristoylphosphatidylcholine lipid bilayers was obtained at 10 degrees C. Oriented lipid multilayers were used to obtain high signal-to-noise intensity data. The chain tilt angle and an estimate of the methylene electron density were obtained from wide angle reflections. The chain tilt angle is measured to be 32.3 +/- 0.6 degrees near full hydration, and it does not change as the sample is mildly dehydrated from a repeat spacing of D = 59.9 A to D = 56.5 A. Low angle diffraction peaks were obtained up to the tenth order for 17 samples with variable D and prepared by three different methods with different geometries. In addition to the usual Fourier reconstructions of the electron density profiles, model electron density profiles were fit to all the low angle data simultaneously while constraining the model to include the wide-angle data and the measured lipid volume. Results are obtained for area/lipid (A = 47.2 +/- 0.5 A(2)), the compressibility modulus (K(A) = 500 +/- 100 dyn/cm), various thicknesses, such as the hydrocarbon thickness (2D(C) = 30.3 +/- 0.2 A), and the head-to-head spacing (D(HH) = 40.1 +/- 0.1 A). 相似文献
3.
Determining bilayer hydrocarbon thickness from neutron diffraction measurements using strip-function models. 总被引:1,自引:3,他引:1
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Neutron diffraction methods provide information about the distribution of matter in biological and model membrane systems. The information is derived from plots (profiles) of scattering length density along an axis normal to the membrane plane. Without the use of specific deuteration, the generally low resolution of the profiles limits their interpretation in terms of specific chemical constituents (e.g., lipid headgroup, lipid hydrocarbon, protein, and water). A fundamental and useful structural assignment to make is the boundary between the headgroup and hydrocarbon regions of bilayers. We demonstrate here that strip-function model representations of neutron scattering length density profiles of bilayers are sufficient to determine accurately the position of the headgroup-hydrocarbon boundary. The resulting hydrocarbon thickness of the bilayer is useful for determining the area per lipid molecule and consequently the molecular packing arrangements of the membrane constituents. We analyze data obtained from dioleoylphosphatidylcholine (DOPC) bilayers at 66% RH using standard Fourier profile analyses and from DOPC deuterated specifically at the C-2 carbon of the acyl chains using difference Fourier analysis. We demonstrate that strip-function models accurately define the positions of the C-2 carbons and thus the hydrocarbon thickness (dhc) of the bilayer. We then show, using quasi-molecular models, that the strip-model analysis probably provides an accurate measure of dhc because of the exceptionally high scattering length density difference between the carbonyl and methylene groups. 相似文献
4.
X-ray structure determination of fully hydrated L alpha phase dipalmitoylphosphatidylcholine bilayers. 总被引:11,自引:7,他引:4
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J F Nagle R Zhang S Tristram-Nagle W Sun H I Petrache R M Suter 《Biophysical journal》1996,70(3):1419-1431
Bilayer form factors obtained from x-ray scattering data taken with high instrumental resolution are reported for multilamellar vesicles of L alpha phase lipid bilayers of dipalmitoylphosphatidylcholine at 50 degrees C under varying osmotic pressure. Artifacts in the magnitudes of the form factors due to liquid crystalline fluctuations have been eliminated by using modified Caillé theory. The Caillé fluctuation parameter eta 1 increases systematically with increasing lamellar D spacing and this explains why some higher order peaks are unobservable for the larger D spacings. The corrected form factors fall on one smooth continuous transform F(q); this shows that the bilayer does not change shape as D decreases from 67.2 A (fully hydrated) to 60.9 A. The distance between headgroup peaks is obtained from Fourier reconstruction of samples with four orders of diffraction and from electron density models that use 38 independent form factors. By combining these results with previous gel phase results, area AF per lipid molecule and other structural quantities are obtained for the fluid L alpha phase. Comparison with results that we derived from previous neutron diffraction data is excellent, and we conclude from diffraction studies that AF = 62.9 +/- 1.3 A2, which is in excellent agreement with a previous estimate from NMR data. 相似文献
5.
R P Mason R F Jacob M F Walter P E Mason N A Avdulov S V Chochina U Igbavboa W G Wood 《The Journal of biological chemistry》1999,274(26):18801-18807
The effects of soluble and aggregated amyloid beta-peptide (Abeta) on cortical synaptic plasma membrane (SPM) structure were examined using small angle x-ray diffraction and fluorescence spectroscopy approaches. Electron density profiles generated from the x-ray diffraction data demonstrated that soluble and aggregated Abeta1-40 peptides associated with distinct regions of the SPM. The width of the SPM samples, including surface hydration, was 84 A at 10 degrees C. Following addition of soluble Abeta1-40, there was a broad increase in electron density in the SPM hydrocarbon core +/-0-15 A from the membrane center, and a reduction in hydrocarbon core width by 6 A. By contrast, aggregated Abeta1-40 contributed electron density to the phospholipid headgroup/hydrated surface of the SPM +/-24-37 A from the membrane center, concomitant with an increase in molecular volume in the hydrocarbon core. The SPM interactions observed for Abeta1-40 were reproduced in a brain lipid membrane system. In contrast to Abeta1-40, aggregated Abeta1-42 intercalated into the lipid bilayer hydrocarbon core +/-0-12 A from the membrane center. Fluorescence experiments showed that both soluble and aggregated Abeta1-40 significantly increased SPM bulk and protein annular fluidity. Physico-chemical interactions of Abeta with the neuronal membrane may contribute to mechanisms of neurotoxicity, independent of specific receptor binding. 相似文献
6.
Reconstruction and interpretation of lipid bilayer structure from X-ray scattering often rely on assumptions regarding the molecular distributions across the bilayer. It is usually assumed that changes in head-head spacings across the bilayer, as measured from electron density profiles, equal the variations in hydrocarbon thicknesses. One can then determine the structure of a bilayer by comparison to the known structure of a lipid with the same headgroup. Here we examine this procedure using simulated electron density profiles for the benchmark lipids DMPC and DPPC. We compare simulation and experiment in both real and Fourier space to address two main aspects: (i) the measurement of head-head spacings from relative electron density profiles, and (ii) the determination of the absolute scale for these profiles. We find supporting evidence for the experimental procedure, thus explaining the robustness and consistency of experimental structural results derived from electron density profiles. However, we also expose potential pitfalls in the Fourier reconstruction that are due to the limited number of scattering peaks. Volumetric analysis of simulated bilayers allows us to propose an improved, yet simple method for scale determination. In this way we are able to remove some of the restrictions imposed by limited scattering data in constructing reliable electron density profiles. 相似文献
7.
X-ray and neutron diffraction methods provide some information about the distribution of mass in biological membranes and lipid-water systems. Scattering density profiles obtained from these systems, however, usually are not directly interpretable in terms of the relative amounts of chemical constituents (e.g., lipid, protein, and water) as a function of position in the membrane. We demonstrate here that the combined use of x-ray and neutron-scattering profiles, together with information on the total amounts of each of the major membrane components, are sufficient to calculate unambiguously the volume fractions of these components at well-defined regions of the lamellar unit. Three cases are considered: a calculated model membrane pair, dipalmitoylphosphatidylcholine-water multilayers, and rabbit sciatic nerve myelin. For the model system, we discuss the limitations imposed by finite resolution in the diffraction patterns. For the lipid-water multilayers, we calculate water volume fractions in the hydrocarbon tail, lipid headgroup, and interlamellar regions; estimates of these values by various methods are in good agreement with our results. For the nerve myelin, we predict new results for the distribution of protein through the membrane. 相似文献
8.
Bringezu F Majerowicz M Wen S Reuther G Tan KT Kuhlmann J Waldmann H Huster D 《European biophysics journal : EBJ》2007,36(4-5):491-498
The adsorption of doubly lipidated full-length N-Ras protein on 1,2-dipalmitoyl-sn-phosphatidylcholine (DPPC) monolayers was studied by lateral pressure analysis, grazing incidence X-ray diffraction (GIXD),
and specular reflectivity (XR). N-Ras protein adsorbs to the DPPC monolayer (lateral pressure of 20 mN/m) from the subphase
thereby increasing the lateral pressure in the monolayer by 4 mN/m. The protein insertion does not alter the tilt angle and
structure of the lipid molecules at the air/water interface but influences the electron density profile of the monolayer.
Further, electron density differences into the subphase were observed. The Fresnel normalized reflectivity could be reconstructed
in the analysis using box models yielding electron density profiles of the DPPC monolayer in the absence and in the presence
of N-Ras protein. The electron density profiles of the DPPC monolayer in the presence of Ras showed clear intensity variations
in the headgroup/glycerol/upper chain region, the so-called interface region where previous bilayer studies had confirmed
Ras binding.
Dedicated to Prof. K. Arnold on the occasion of his 65th birthday. 相似文献
9.
Keith M. Meek Gerald F. Elliott Zehra Sayers Susan B. Whitburn Michel H.J. Koch 《Journal of molecular biology》1981,149(3):477-488
The low angle X-ray diffraction pattern from corneal stroma can be interpreted as arising from the equivalent of sharp meridional reflections due to the packing of molecules along the collagen fibrils and an equatorial pattern due to the packing of these fibrils within lamellae.Axial electron density profiles for corneal collagen fibrils have been produced by combining intensity data from the meridional pattern with two independent sets of phases. The first set was obtained using an electron microscopical technique, whereas the second set consisted of calculated tendon collagen phases given in the literature. Substantial agreement between the two electron density profiles was found.A quantitative analysis of the difference between the electron density profiles of rat tail tendon and corneal collagen showed that the step between the gap and overlap regions is smaller in cornea than in tendon. This is probably due to the binding of non-collagenous material in the gap region as occurs in bone and other tissue. Two peaks corresponding to regions where electron density is greater in the cornea are situated at the gap/overlap junctions. A third region where the corneal collagen is more electron dense is located near the centre of the gap region. The proximity of these peaks to the positions of hydroxylysine residues along the fibril axis suggests that they may be the major sites at which sugars are bound to corneal collagen. 相似文献
10.
山莨菪碱与膜相互作用的小角X射线衍射研究 总被引:1,自引:0,他引:1
应用小角X射线衍射和差示扫描量热法研究了中药提取物山莨菪碱与DPPC多层膜的相互作用.结果表明,山莨菪碱不仅能降低DPPC多层膜的相变温度,而且能使多层膜发生分相现象,根据衍射结果并采用推广傅里叶合成去卷积法计算了脂双分子层膜的电子密度剖面图.从中我们估计山莨菪碱分子可能分布于脂双分子层极性头部的内侧 相似文献
11.
Amiodarone, a potent antiarrhythmic drug, is widely used in cardiology. Its electrophysiological effects, as well as many of its side effects, seem to involve lipids. We report here a multinuclear NMR and X-ray diffraction study of amiodarone in egg phosphatidylcholine liposomes and lipid multilayers. In proton NMR experiments, amiodarone alters the signal from the lipid trimethyl ammonium group for pH values ranging from 3.2 to 8.4; cholesterol does not cause this alteration. The addition of SCN- changes both the proton and phosphorus NMR spectra of liposomes containing amiodarone. For both proton and carbon NMR, amiodarone modifies the signal from the lipid methylene groups, but to a far lesser extent than does cholesterol. Incorporation of amiodarone in EPC bilayers also modifies the low-angle X-ray diffraction patterns, decreasing the lamellar repeat period at low water contents, but swelling the fluid spaces between bilayers at high water contents. Electron density profiles and modeling studies using the X-ray data indicate that amiodarone decreases the bilayer thickness and adds electron density at the interfacial region of the bilayer. Our analysis of the NMR and X-ray data indicates that the iodine atoms of amiodarone are located near the hydrocarbon/water interface and that the tertiary amine of amiodarone is in the headgroup region of the bilayer. 相似文献
12.
Myelin labeled with mercuric chloride. Asymmetric localization of phosphatidylethanolamine plasmalogen 总被引:5,自引:0,他引:5
We have recorded modified X-ray diffraction patterns to 15 Å spacing from sciatic nerves treated with mercuric chloride (HgCl2) at concentrations of 0.5 to 32 mm in water or in saline. The observed changes in repeat period and in the intensities of the low-order reflections indicate closer packing of membranes at their cytoplasmic surfaces after treatments with HgCl2. In addition, HgCl2 at 0.25 mm or more prevents swelling in water at the extracellular boundaries. By comparing the distinctive diffraction patterns from nerves treated under different conditions with HgCl2, we have interpreted the changes in intensities of the higher order X-ray reflections and have calculated electron density profiles of the modified membranes. The most striking difference between membrane profiles before and after treatment with HgCl2 is the large increase in electron density in the region of the lipid headgroup peak in the cytoplasmic half of the bilayer. The magnitude and location of this increase suggests labeling of myelin lipid. To examine this possibility, we analyzed the lipids from mercury-treated sciatic nerves.Thin-layer chromatography of lipids extracted from nerves treated with HgCl2 shows a marked decrease of phosphatidylethanolamine, which exists in myelin primarily as plasmalogen. At the same time, a new spot identified as lysophosphatidylethanolamine appears. An identical result was obtained by treating extracted lipids with HgCl2, suggesting that the same sites of interaction are present in the intact membrane as in the dispersed lipids. Previous studies on plasmalogens indicate that mercury adds to the β-carbon of the α,β-unsaturated ether group to produce a lyso-lipid and an aldehyde with bound mercury (Norton, 1959). From a correlation of our X-ray structural analysis and the chemical studies, we conclude that phosphatidylethanolamine plasmalogen is preferentially localized in the cytoplasmic half of the myelin membrane bilayer. 相似文献
13.
Ferrochelatase activity in wild-type and mutant strains of Spirillum itersonii. Solubilization with chaotropic reagents 总被引:5,自引:0,他引:5
New low-angle X-ray diffraction data have been obtained from nerve myelin after rehydration. The X-ray patterns show the first six orders of diffraction of a lamellar repeat unit of about 100 Å. Direct methods of structure analysis have been used to determine uniquely the phases of the first three orders of diffraction. The electron density profile of rehydrated nerve myelin has been obtained on an absolute electron density scale and is compared with the electron density profile of normal nerve myelin at the same resolution of 16–17 Å. Possible electron-density profiles of rehydrated nerve myelin at a resolution of 8 Å are shown. 相似文献
14.
Changes in the sarcoplasmic reticulum membrane profile induced by enzyme phosphorylation to E1 approximately P at 16 A resolution via time-resolved x-ray diffraction. 总被引:2,自引:2,他引:0
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D Pascolini L G Herbette V Skita F Asturias A Scarpa J K Blasie 《Biophysical journal》1988,54(4):679-687
Time-resolved x-ray diffraction studies of the isolated sarcoplasmic reticulum (SR) membrane have provided the difference electron density profile for the SR membrane for which the Ca2+ ATPase is transiently trapped exclusively in the first phosphorylated intermediate state, E1 approximately P, in absence of detectable enzyme turnover vs. that before ATP-initiated phosphorylation of the enzyme. These diffraction studies, which utilized the flash-photolysis of caged ATP, were performed at temperatures between 0 and -2 degrees C and with a time-resolution of 2-5 s. Analogous time-resolved x-ray diffraction studies of the SR membrane at 7-8 degrees C with a time resolution of 0.2-0.5 s have previously provided the difference electron density profile for the SR membrane for which the Ca2+ ATPase is only predominately in the first phosphorylated intermediate state under conditions of enzyme turnover vs. that before enzyme phosphorylation. The two difference profiles, compared at the same low resolution (approximately 40 A), are qualitatively similar but nevertheless contain some distinctly different features and have therefore been analyzed via a step-function model analysis. This analysis was based on the refined step-function models for the two different electron density profiles obtained independently from x-ray diffraction studies at higher resolution (16-17 A) of the SR membrane before enzyme phosphorylation at 7.5 and -2 degrees C. The step-function model analysis indicated that the low resolution difference profiles derived from both time-resolved x-ray diffraction experiments arise from a net movement of Ca2+ ATPase protein mass from the outer monolayer to the inner monolayer of the SR membrane lipid bilayer.(ABSTRACT TRUNCATED AT 250 WORDS) 相似文献
15.
Location of high-affinity metal binding sites in the profile structure of the Ca+2-ATPase in the sarcoplasmic reticulum by resonance x-ray diffraction. 总被引:3,自引:3,他引:0
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Resonance x-ray diffraction measurements on the lamellar diffraction from oriented multilayers of isolated sarcoplasmic reticulum (SR) membranes containing a small concentration of lanthanide (III) ions (lanthanide/protein molar ratio approximately 4) have allowed us to calculate both the electron density profile of the SR membrane and the separate electron density profile of the resonant lanthanide atoms bound to the membrane to a relatively low spatial resolution of approximately 40 A. Analysis of the membrane electron density profile and modeling of the separate low resolution lanthanide atom profile, using step-function electron density models based on the assumption that metal binding sites in the membrane profile are discrete and localized, resulted in the identification of a minimum of three such binding sites in the membrane profile. Two of these sites are low-affinity, low-occupancy sites identified with the two phospholipid polar headgroup regions of the lipid bilayer within the membrane profile. Up to 20% of the total lanthanide (III) ions bind to these low-affinity sites. The third site has relatively high affinity for lanthanide ion binding; its Ka is roughly an order of magnitude larger than that for the lower affinity polar headgroup sites. Approximately 80% of the total lanthanide ions present in the sample are bound to this high-affinity site, which is located in the "stalk" portion of the "headpiece" within the profile structure of the Ca+2 ATPase protein, approximately 12 A outside of the phospholipid polar headgroups on the extravesicular side of the membrane profile. Based on the nature of our results and on previous reports in the literature concerning the ability of lanthanide (III) ions to function as Ca+2 analogues for the Ca+2 ATPase we suggest that we have located a high-affinity metal binding site in the membrane profile which is involved in the active transport of Ca+2 ions across the SR membrane by the Ca+2 ATPase. 相似文献
16.
Axial electron density of human scleral collagen. Location of proteoglycans by x-ray diffraction.
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The low angle meridional x-ray diffraction pattern from fresh human sclera was analyzed to ascertain if collagen-bound proteoglycans affect the axially-projected electron density distribution to the same extent as appears to occur in the cornea. The results showed that, unlike cornea, the electron density of the sclera is similar to that seen in rat tail tendon collagen. The proteoglycans were specifically stained using either Cuprolinic blue or Cupromeronic blue, both under critical electrolyte conditions. The tissue was then examined by electron microscopy and by low angle x-ray diffraction. The electron-optical observations suggested that proteoglycans associate with collagen near the d/e staining bands in the gap zone. A difference Fourier analysis from the x-ray results confirmed that these observations were not e.m. preparative artefacts and allowed a quantitative estimate to be made of the axial extent of the proteglycans in the wet tissue. 相似文献
17.
K. Pande P. Schwander M. Schmidt D. K. Saldin 《Philosophical transactions of the Royal Society of London. Series B, Biological sciences》2014,369(1647)
We propose a method for deducing time-resolved structural changes in uncrystallized biomolecules in solution. The method relies on measuring the angular correlations of the intensities, when averaged over a large number of diffraction patterns from randomly oriented biomolecules in solution in a liquid solvent. The experiment is somewhat like a pump–probe version of an experiment on small angle X-ray scattering, except that the data expected by the algorithm are not just the radial variation of the averaged intensities. The differences of these correlation functions as measured from a photoexcited and dark structure enable the direct calculation of the difference electron density with a knowledge of only the dark structure. We exploit a linear relation we derive between the difference in these correlation functions and the difference electron density, applicable for small structural changes. 相似文献
18.
Sequences of X-ray diffraction patterns were obtained from dehydrating, artificially oriented multilayers of isolated, bovine rod outer segment disks. A direct-phase analysis was applied to highly hydrated specimens to determine sequences of low resolution (approx. 30 Å) electron density profiles of the disks as dehydration proceeded. The profiles were found to evolve smoothly as the multilayer lattice simultaneously shrank and became increasingly ordered. The bilayer profiles were largely invariant under dehydration and the evolution of the diffraction consistent with simple decreases in fluid spacings. The specimens were observed to phase separate into characteristic primary and a secondary lattices when the multi-layer became too dehydrated. The small unit cell size of the secondary lattice was suggestive of a lipid phase. Large changes in the diffraction patterns from phase separated specimens were observed upon bleaching of the specimen. The changes were consistent with a reversible disordering of the primary lattice. 相似文献
19.
Phosphatidylinositol (PI) bilayers, squeezed together by applied osmotic pressures, were studied by both neutron diffraction and X-ray diffraction. The lamellar repeat period for PI bilayers decreased from 9.5 nm at an applied pressure of 1.1.10(6) dyn/cm2 (1.1 atm) to 5.4 nm at an applied pressure of 1.6.10(7) dyn/cm2 (16 atm). Further increases in applied pressure, up to 2.7.10(9) dyn/cm2 (2700 atm) reduced the repeat period by only about 0.3 nm, to 5.1 nm. Thus, a plot of applied pressure versus repeat period shows a sharp upward break for repeat periods less than about 5.4 nm. For repeat periods of less than 5.4 nm, analysis of neutron-scattering density profiles and electron-density profiles indicates that the structure of the PI bilayers changes as the bilayers are dehydrated, even though there are only small changes in the repeat period. These structural changes are most likely due to removal of water from the headgroup regions of the bilayer. D2O/H2O exchange experiments show that, at an applied pressure of 2.8.10(7) dyn/cm2, water is located between adjacent PI headgroups in the plane of the bilayer. We conclude that, although electrostatics provide the dominant long-range repulsive interaction, hydration repulsion and steric hindrance between PI headgroups from apposing bilayers provide the major barriers for the close approach of adjacent PI bilayers for repeat periods less than 5.4 nm. This structural analysis also indicates that the phosphoinositol group extends from the plane of the bilayer into the fluid space between adjacent bilayers. This extended orientation for the headgroup is consistent with electrophoretic measurements on PI vesicles. 相似文献
20.
Study of phospholipid structure by 1H, 13C, and 31P dipolar couplings from two-dimensional NMR.
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Various motionally averaged 31P-1H, 13C-1H, 1H-1H, and 31P-13C dipolar couplings were measured for natural-abundance and unoriented phosphocholine in the L alpha phase. The couplings were obtained and assigned by a variety of advanced and partly novel two-dimensional solid-state NMR experiments. Whereas 31P-1H and 31P-13C dipolar couplings provide long-range structural constraints, geminal 1H-1H couplings and the signs of 13C-1H couplings are important new elements in a segmental order-tensor analysis of the lipid headgroup and glycerol backbone. The implications of these measured dipolar couplings for the conformational exchange of the lipid headgroup and the bending of the headgroup from the glycerol backbone are discussed. These dipolar couplings are also analyzed semiquantitatively in terms of the segmental order tensor. 相似文献