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2.
Phys Rev Lett ; 121(5): 051301, 2018 Aug 03.
Article in English | MEDLINE | ID: mdl-30118251

ABSTRACT

We present the first limits on inelastic electron-scattering dark matter and dark photon absorption using a prototype SuperCDMS detector having a charge resolution of 0.1 electron-hole pairs (CDMS HVeV, a 0.93Ā g CDMS high-voltage device). These electron-recoil limits significantly improve experimental constraints on dark matter particles with masses as low as 1 MeV/c^{2}. We demonstrate a sensitivity to dark photons competitive with other leading approaches but using substantially less exposure (0.49Ā gĀ d). These results demonstrate the scientific potential of phonon-mediated semiconductor detectors that are sensitive to single electronic excitations.

3.
Phys Rev Lett ; 120(6): 061802, 2018 Feb 09.
Article in English | MEDLINE | ID: mdl-29481237

ABSTRACT

We report the result of a blinded search for weakly interacting massive particles (WIMPs) using the majority of the SuperCDMS Soudan data set. With an exposure of 1690Ā kg d, a single candidate event is observed, consistent with expected backgrounds. This analysis (combined with previous Ge results) sets an upper limit on the spin-independent WIMP-nucleon cross section of 1.4Ɨ10^{-44} (1.0Ɨ10^{-44}) cm^{2} at 46 GeV/c^{2}. These results set the strongest limits for WIMP-germanium-nucleus interactions for masses >12 GeV/c^{2}.

4.
Phys Rev Lett ; 116(7): 071301, 2016 Feb 19.
Article in English | MEDLINE | ID: mdl-26943526

ABSTRACT

The CDMS low ionization threshold experiment (CDMSlite) uses cryogenic germanium detectors operated at a relatively high bias voltage to amplify the phonon signal in the search for weakly interacting massive particles (WIMPs). Results are presented from the second CDMSlite run with an exposure of 70Ā kg day, which reached an energy threshold for electron recoils as low as 56Ā eV. A fiducialization cut reduces backgrounds below those previously reported by CDMSlite. New parameter space for the WIMP-nucleon spin-independent cross section is excluded for WIMP masses between 1.6 and 5.5 GeV/c^{2}.

5.
Phys Rev Lett ; 114(11): 111302, 2015 Mar 20.
Article in English | MEDLINE | ID: mdl-25839256

ABSTRACT

While the standard model of particle physics does not include free particles with fractional charge, experimental searches have not ruled out their existence. We report results from the Cryogenic Dark Matter Search (CDMS II) experiment that give the first direct-detection limits for cosmogenically produced relativistic particles with electric charge lower than e/6. A search for tracks in the six stacked detectors of each of two of the CDMS II towers finds no candidates, thereby excluding new parameter space for particles with electric charges between e/6 and e/200.

6.
Phys Rev Lett ; 112(4): 041302, 2014 Jan 31.
Article in English | MEDLINE | ID: mdl-24580434

ABSTRACT

SuperCDMS is an experiment designed to directly detect weakly interacting massive particles (WIMPs), a favored candidate for dark matter ubiquitous in the Universe. In this Letter, we present WIMP-search results using a calorimetric technique we call CDMSlite, which relies on voltage-assisted Luke-Neganov amplification of the ionization energy deposited by particle interactions. The data were collected with a single 0.6Ā kg germanium detector running for ten live days at the Soudan Underground Laboratory. A low energy threshold of 170 eVee (electron equivalent) was obtained, which allows us to constrain new WIMP-nucleon spin-independent parameter space for WIMP masses below 6 GeV/c2.

7.
Phys Rev Lett ; 112(24): 241302, 2014 Jun 20.
Article in English | MEDLINE | ID: mdl-24996080

ABSTRACT

We report a first search for weakly interacting massive particles (WIMPs) using the background rejection capabilities of SuperCDMS. An exposure of 577 kg days was analyzed for WIMPs with mass <30 GeV/c(2), with the signal region blinded. Eleven events were observed after unblinding. We set an upper limit on the spin-independent WIMP-nucleon cross section of 1.2Ɨ10(-42) cm(2) at 8 GeV/c(2). This result is in tension with WIMP interpretations of recent experiments and probes new parameter space for WIMP-nucleon scattering for WIMP masses <6 GeV/c(2).

8.
Phys Rev Lett ; 111(25): 251301, 2013 Dec 20.
Article in English | MEDLINE | ID: mdl-24483735

ABSTRACT

We report results of a search for weakly interacting massive particles (WIMPS) with the silicon detectors of the CDMS II experiment. This blind analysis of 140.2 kg day of data taken between July 2007 and September 2008 revealed three WIMP-candidate events with a surface-event background estimate of 0.41(-0.08)(+0.20)(stat)(-0.24)(+0.28)(syst). Other known backgrounds from neutrons and 206Pb are limited to <0.13 and <0.08 events at the 90% confidence level, respectively. The exposure of this analysis is equivalent to 23.4 kg day for a recoil energy range of 7-100 keV for a WIMP of mass 10 GeV/c2. The probability that the known backgrounds would produce three or more events in the signal region is 5.4%. A profile likelihood ratio test of the three events that includes the measured recoil energies gives a 0.19% probability for the known-background-only hypothesis when tested against the alternative WIMP+background hypothesis. The highest likelihood occurs for a WIMP mass of 8.6 GeV/c2 and WIMP-nucleon cross section of 1.9Ɨ10(-41) cm2.

9.
Biosens Bioelectron ; 23(7): 1161-5, 2008 Feb 28.
Article in English | MEDLINE | ID: mdl-18054481

ABSTRACT

This report describes the fabrication and successful use of the ion channel switch biosensor (ICSB) for rapid point-of-care detection of influenza A in different types of respiratory specimens. Virus culture -- regarded as the "gold standard" -- and an immunochromatographic rapid point-of-care test for influenza A virus were compared with the biosensor. The ICSB rapid test provided an objective readout within 10 min of specimen inoculation into the ICSB chamber wells, without the need for chemical or other pretreatments. Construction of the ICSB with specific antibodies also enables rapid detection and identification of appropriate influenza A subtypes.


Subject(s)
Biosensing Techniques/instrumentation , Immunoassay/instrumentation , Influenza A virus/isolation & purification , Viral Load/instrumentation , Biosensing Techniques/methods , Computer Systems , Equipment Design , Equipment Failure Analysis , Humans , Immunoassay/methods , Ions , Reproducibility of Results , Sensitivity and Specificity , Viral Load/methods
10.
Biochim Biophys Acta ; 1278(2): 160-8, 1996 Jan 31.
Article in English | MEDLINE | ID: mdl-8593272

ABSTRACT

31P electric field nuclear magnetic resonance measurements are described which assess the effect of electric field on the orientation of tubules comprising the HII phase of dioeleoylphosphatidylethanolamine. A model, based on dielectrophoretic effects, was used to predict that a field of 4 MV/m would change the orientation of the lipid tubules in a HII phase. The excitation pulse was biphasic to help discriminate electric field interactions with free ions or permanent dipoles from interactions with induced dipoles, as well as to control the problems of ohmic heating, electrolysis and polarisation associated with dc or unbalanced ac excitation voltages. Spectra consistent with irreversible electrorotation and with reversible and transient electrorotation were observed. No response to the electric field was seen in certain cases. The conditions for irreversible and reversible electrorotation and failure to rotate have been tabulated and are discussed. Finally, some simple models are considered, in order to calculate the energies involved, if the observed NMR spectra are interpreted as arising from lipid HII phase reorientations.


Subject(s)
Magnetic Resonance Spectroscopy , Phosphatidylethanolamines/chemistry , Electric Impedance , Electricity , Electrophoresis , Mathematics , Phosphorus Isotopes , Thermodynamics
11.
Biochim Biophys Acta ; 1195(2): 197-204, 1994 Nov 02.
Article in English | MEDLINE | ID: mdl-7947910

ABSTRACT

A technique is described for measuring the effect of electric fields on the conformation of lipid bilayer membranes by solid state nuclear magnetic resonance. An apparatus was devised to obtain spectra from samples of aligned phospholipid dispersions at varying electric field strengths up to 100 MV/m. Measurements were carried out on membranes made from dioleoylphosphatidylethanolamine and dioleoylphosphatidylcholine, which resulted in electric field induced phase changes. Calibration experiments were performed using bilayers formed from dimyristoylphosphatidylcholine with glycerol and with a nematic liquid crystal. An electric field induced change, from L alpha to HII, was also seen in a dimyristoylphosphatidylcholine/alamethicin bilayer.


Subject(s)
Lipid Bilayers/chemistry , Electricity , Magnetic Resonance Spectroscopy , Molecular Conformation , Phosphorus Isotopes
12.
Biochim Biophys Acta ; 818(2): 275-9, 1985 Aug 27.
Article in English | MEDLINE | ID: mdl-2411291

ABSTRACT

31P nuclear magnetic resonance and low-angle X-ray diffraction measurements have shown that the basic protein of myelin caused diacylphosphatidic acid dispersions to change from a lamellar to a hexagonal lipid organisation. Several other basic proteins failed to effect a similar phase change, and had little influence on phospholipid headgroup structure and motion.


Subject(s)
Myelin Basic Protein , Phosphatidic Acids , Chemical Phenomena , Chemistry , Hydrogen-Ion Concentration , Magnetic Resonance Spectroscopy , Thermodynamics , X-Ray Diffraction
13.
Biochim Biophys Acta ; 733(1): 189-93, 1983 Aug 24.
Article in English | MEDLINE | ID: mdl-6882754

ABSTRACT

It appears reasonable to expect that the primary result of a change in the length of the acyl chains within a lipid bilayer is a similar change in the bilayer thickness. In the present communication we draw attention to the somewhat more complicated effects which are found experimentally for phosphatidylcholine bilayers as the hydrocarbon chain is varied from twelve to eighteen carbons in length. The major change in dimension which occurs with variation in acyl chain length is the area occupied per molecule rather than the bilayer thickness. The same effect is seen with solute hydrocarbon such as hexane which partition into the membrane and cause only a small variation in membrane thickness but a large increase in the molecular area of the lipid. The origin of this effect arises from the almost isotropic distribution of the additional hydrocarbon to the lipid core of the membrane.


Subject(s)
Lipid Bilayers , Phosphatidylcholines , Fatty Acids , Molecular Conformation , Structure-Activity Relationship , X-Ray Diffraction
14.
Biochim Biophys Acta ; 689(2): 337-45, 1982 Jul 28.
Article in English | MEDLINE | ID: mdl-6180764

ABSTRACT

Nuclear magnetic resonance (NMR) relaxation techniques have been used to study the effect of lipid-protein interactions on the dynamics of membrane lipids. Proton enhanced (PE) 13C-NMR measurements are reported for the methylene chain resonances in red blood cell membranes and their lipid extracts. For comparison similar measurements have been made of phospholipid dispersions containing cholesterol and the polypeptide gramicidin A+. It is found that the spin-lattice relaxation time in the rotating reference frame (T1 rho) is far more sensitive to protein, gramicidin A+ or cholesterol content than is the laboratory frame relaxation time (T1). Based on this data it is concluded that the addition of the second component to a lipid bilayer produces a low-frequency motion in the region of 10(5) to 10(7) Hz within the membrane lipid. The T1 rho for the superimposed resonance peaks derived from all parts of the phospholipid chain are all influenced in the same manner suggesting that the low frequency motion involves collective movements of large segments of the hydrocarbon chain. Because of the molecular co-operativity implied in this type of motion and the greater sensitivity of T1 rho to the effects of lipid-protein interactions generally, it is proposed that these low-frequency perturbations are felt at a greater distance from the protein than those at higher frequencies which dominate T1.


Subject(s)
Cholesterol , Erythrocyte Membrane/ultrastructure , Erythrocytes/ultrastructure , Gramicidin , Lipid Bilayers , Membrane Lipids/blood , Membrane Proteins/blood , Dimyristoylphosphatidylcholine , Humans , Kinetics , Magnetic Resonance Spectroscopy , Molecular Conformation , Phosphatidylcholines/blood , Protein Conformation , Temperature
15.
Biochim Biophys Acta ; 598(2): 405-10, 1980 May 23.
Article in English | MEDLINE | ID: mdl-7378411

ABSTRACT

It is shown that the area occupied per phospholipid molecule and the thickness of the bilayer are the same in vesicles as in a planar bilayer. From this it is concluded thtat the lower limit to the size of a vesicle depends on the packing of the head groups of the inner monolayer.


Subject(s)
Lipid Bilayers , Phosphatidylcholines , Hydrogen Bonding , Molecular Conformation , Molecular Weight , Surface Properties , Thermodynamics
16.
Biochim Biophys Acta ; 862(2): 451-6, 1986 Nov 17.
Article in English | MEDLINE | ID: mdl-3022812

ABSTRACT

The 31P nuclear magnetic resonance anisotropies of dispersions of diacylphosphatidic acid and diacylphosphatidylserine were slightly increased in the presence of cytochrome c: no increase was observed with cardiolipin. However, the 31P spin-lattice relaxation times (T1) for all of these lipids were reduced markedly by the protein. As similar effects were observed with ferri-cytochrome c and with the reduced protein, which is diamagnetic, we suggest that the changes in T1 reflect a reduction in the spectral density of fast motions for the lipid headgroups attendant on binding of protein, rather than paramagnetic relaxation of the phosphorus nuclear spin.


Subject(s)
Cytochrome c Group/metabolism , Liposomes , Animals , Horses , Kinetics , Magnetic Resonance Spectroscopy/methods , Myocardium/metabolism , Oxidation-Reduction , Phosphorus
17.
Biochim Biophys Acta ; 732(3): 492-8, 1983 Aug 10.
Article in English | MEDLINE | ID: mdl-6191774

ABSTRACT

Lysozyme, cytochrome c, poly(L-lysine), myelin basic protein and ribonuclease were used to form multilayer dispersions containing about 50% protein (by weight) with bovine brain diacyl phosphatidylserine (PS). 31P nuclear magnetic resonance shift anisotropies, spin-spin (T2) and spin-lattice (T1) relaxation times for the lipid headgroup phosphorus were measured at 36.44 MHz. At pH 7.5, lysozyme, cytochrome c, poly(L-lysine) and ribonuclease were shown to increase the chemical shift anisotropy of PS by between 12-20%. Myelin basic protein altered the shape of the phosphate resonance, suggesting the presence of two lipid components, one of which had a modified headgroup conformation. The presence of cytochrome c led to the formation of a narrow spike at the isotropic shift position of the spectrum. Of the various proteins or peptides we have studied, only poly(L-lysine) and cytochrome c had any effect on the T1 of PS (1050 ms). Both caused a 20-30% decrease in T1 of the lamellar-phase phosphate peak. The narrow peak in the presence of cytochrome c had a very short T1 of 156 ms. The possibility is considered that the cytochrome Fe3+ contributes to the phosphate relaxation in this case. The effect of all proteins on the T2 of the phosphorus resonance was to cause an increase from the value for pure PS (1.6 ms) to between 2 and 5 ms. The results obtained with proteins are compared with the effects of small ions and intrinsic membrane proteins on the order and motion of the headgroups of lipids in bilayers.


Subject(s)
Liposomes , Myelin Basic Protein/metabolism , Phosphatidylserines/metabolism , Animals , Brain/metabolism , Cattle , Cytochrome c Group/metabolism , Horses , Magnetic Resonance Spectroscopy , Muramidase/metabolism , Myocardium , Polylysine/metabolism
18.
Biochim Biophys Acta ; 690(1): 15-9, 1982 Aug 25.
Article in English | MEDLINE | ID: mdl-7126566

ABSTRACT

The effective hydrodynamic radius of small sonicated phospholipid vesicles has been measured by photon correlation laser light scattering. It is found that the minimum radius obtained for these vesicles is within the range 10.25 +/- 0.55 nm independent of the phospholipid hydrocarbon chain length for synthetic phosphatidylcholines in the even numbered series of 12 to 18 carbons per hydrocarbon chain. The minimum radius of vesicles of egg yolk phosphatidylcholine is 10.7 +/- 0.3 nm.


Subject(s)
Liposomes , Phosphatidylcholines , Lasers , Molecular Conformation , Scattering, Radiation , Structure-Activity Relationship
19.
Biochim Biophys Acta ; 1026(2): 161-6, 1990 Jul 24.
Article in English | MEDLINE | ID: mdl-1696125

ABSTRACT

End-to-end helical dimers of gramicidin A form transmembrane pores in lipid bilayers, through which monovalent ions may pass. The groups within the peptide that interact with these ions have been studied by application of solid-state spectroscopic methods to a series of gramicidin A analogues synthesized with 13C in selected peptide carbonyl groups. The resonances of D-Leu10, D-Leu12 and D-Leu14 analogues were perturbed in the presence of 0.16 M sodium ions, whereas the resonances of the carbonyls of Gly2, Ala3, D-Leu4 and Val7, which are closer to the formylated N-terminal end of the peptide, were unaffected. The observed changes in chemical shift anisotropy are indicative of a change in orientation of the abovementioned leucine carbonyls.


Subject(s)
Gramicidin , Ion Channels/ultrastructure , Sodium/pharmacology , Dimyristoylphosphatidylcholine , In Vitro Techniques , Lipid Bilayers , Magnetic Resonance Spectroscopy , Membrane Lipids , Phosphatidylcholines , Protein Conformation , Structure-Activity Relationship
20.
Biochim Biophys Acta ; 985(2): 229-32, 1989 Oct 16.
Article in English | MEDLINE | ID: mdl-2478193

ABSTRACT

The transmembrane ion transport properties of gramicidin A have previously been shown to dependent on the nature of its lipid environment. Solid-state NMR spectroscopic studies of 13C-labelled analogues of gramicidin in oriented multilayers of phosphatidylcholine have shown that variation of the lipid hydrocarbon chain length has no effect on the structure or orientation of the peptide backbone.


Subject(s)
Gramicidin , Lipid Bilayers , Phosphatidylcholines , Carbon Isotopes , Magnetic Resonance Spectroscopy , Models, Biological , Structure-Activity Relationship
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