scholarly journals Chiral partner structure of heavy baryons from the bound state approach with hidden local symmetry

2013 ◽  
Vol 87 (5) ◽  
Author(s):  
Masayasu Harada ◽  
Yong-Liang Ma
Keyword(s):  
Local Symmetry ◽  
Bound State ◽  
Heavy Baryons ◽  
Chiral Partner

scholarly journals The bound state corrections to the semileptonic decays of the heavy baryons

2003 ◽  
Vol 115 ◽  
pp. 15-19
Author(s):  
I. D'Souza ◽  
C.S. Kalman ◽  
P.Yu. Kulikov ◽  
I.M. Narodetskii
Keyword(s):  
Semileptonic Decays ◽  
Bound State ◽  
Heavy Baryons

DOUBLY HEAVY EXOTICS

2014 ◽  
Vol 35 ◽  
pp. 1460432
Author(s):  
MAREK KARLINER
Keyword(s):  
Experimental Data ◽  
Experimental Evidence ◽  
Light Quark ◽  
Bound State ◽  
Exotic State ◽  
Decay Modes ◽  
Exotic States ◽  
Quantum Numbers ◽  
Heavy Baryons ◽  
Molecular Picture

During the last three years strong experimental evidence from B and charm factories has been accumulating for the existence of exotic hadronic quarkonia, narrow resonances which cannot be made from a quark and an antiquark. Their masses and decay modes show that they contain a heavy quark-antiquark pair, but their quantum numbers are such that they must also contain a light quark-antiquark pair. The main theoretical challenge has been to determine the nature of these resonances. The main possibilities are that they are either "genuine tetraquarks", i.e. two quarks and two antiquarks within one confinement volume, or "hadronic molecules" of two heavy-light mesons. In the last few months there is more and more evidence in favor of the latter. I discuss the experimental data and its interpretation and provide fairly precise predictions for masses and quantum numbers of the additional exotic states which are naturally expected in the molecular picture but have yet to be observed. I also provide arguments in favor of the existence of an even more exotic state – a hypothetical deuteron-like bound state of two heavy baryons.

scholarly journals Excited heavy baryons in the bound state picture

1995 ◽  
Vol 51 (5) ◽  
pp. 2311-2321 ◽  
Author(s):  
Joseph Schechter ◽  
Anand Subbaraman
Keyword(s):  
Bound State ◽  
Heavy Baryons

scholarly journals Doubly heavy baryons with chiral partner structure

2015 ◽  
Vol 748 ◽  
pp. 463-466 ◽  
Author(s):  
Yong-Liang Ma ◽  
Masayasu Harada
Keyword(s):  
Heavy Baryons ◽  
Chiral Partner

ELNES of Iron Compounds

1990 ◽  
Vol 48 (2) ◽  
pp. 28-29
Author(s):  
Hiroki Kurata ◽  
Kazuhiro Nagai ◽  
Seiji Isoda ◽  
Takashi Kobayashi
Keyword(s):  
Energy Loss ◽  
Metal Ions ◽  
Energy Resolution ◽  
Transition Metal Oxides ◽  
Local Symmetry ◽  
Iron Compounds ◽  
Fine Structures ◽  
Electron Energy Loss ◽  
Fe Ions ◽  
Electron Energy Loss Spectra

Electron energy loss spectra of transition metal oxides, which show various fine structures in inner shell edges, have been extensively studied. These structures and their positions are related to the oxidation state of metal ions. In this sence an influence of anions coordinated with the metal ions is very interesting. In the present work, we have investigated the energy loss near-edge structures (ELNES) of some iron compounds, i.e. oxides, chlorides, fluorides and potassium cyanides. In these compounds, Fe ions (Fe2+ or Fe3+) are octahedrally surrounded by six ligand anions and this means that the local symmetry around each iron is almost isotropic.EELS spectra were obtained using a JEM-2000FX with a Gatan Model-666 PEELS. The energy resolution was about leV which was mainly due to the energy spread of LaB6 -filament. The threshole energies of each edges were measured using a voltage scan module which was calibrated by setting the Ni L3 peak in NiO to an energy value of 853 eV.

The limits of strain and lattice parameter measurements by CBED

1989 ◽  
Vol 47 ◽  
pp. 518-519
Author(s):  
Hamish L. Fraser
Keyword(s):  
Electron Beam ◽  
Mirror Symmetry ◽  
Local Symmetry ◽  
Lattice Parameter ◽  
Growth Direction ◽  
Surface Relaxation ◽  
Strained Layer ◽  
Axis Parallel ◽  
Local Lattice ◽  
Strained Layer Superlattice

The topic of strain and lattice parameter measurements using CBED is discussed by reference to several examples. In this paper, only one of these examples is referenced because of the limitation of length. In this technique, scattering in the higher order Laue zones is used to determine local lattice parameters. Work (e.g. 1) has concentrated on a model strained-layer superlattice, namely Si/Gex-Si1-x. In bulk samples, the strain is expected to be tetragonal in nature with the unique axis parallel to [100], the growth direction. When CBED patterns are recorded from the alloy epi-layers, the symmetries exhibited by the patterns are not tetragonal, but are in fact distorted from this to lower symmetries. The spatial variation of the distortion close to a strained-layer interface has been assessed. This is most readily noted by consideration of Fig. 1(a-c), which show enlargements of CBED patterns for various locations and compositions of Ge. Thus, Fig. 1(a) was obtained with the electron beam positioned in the center of a 5Ge epilayer and the distortion is consistent with an orthorhombic distortion. When the beam is situated at about 150 nm from the interface, the same part of the CBED pattern is shown in Fig. 1(b); clearly, the symmetry exhibited by the mirror planes in Fig. 1 is broken. Finally, when the electron beam is positioned in the center of a 10Ge epilayer, the CBED pattern yields the result shown in Fig. 1(c). In this case, the break in the mirror symmetry is independent of distance form the heterointerface, as might be expected from the increase in the mismatch between 5 and 10%Ge, i.e. 0.2 to 0.4%, respectively. From computer simulation, Fig.2, the apparent monocline distortion corresponding to the 5Ge epilayer is quantified as a100 = 0.5443 nm, a010 = 0.5429 nm and a001 = 0.5440 nm (all ± 0.0001 nm), and α = β = 90°, γ = 89.96 ± 0.02°. These local symmetry changes are most likely due to surface relaxation phenomena.

CRYO-Electron Microscopy of the Acto-Myosin-ATP Complex

1990 ◽  
Vol 48 (1) ◽  
pp. 248-249
Author(s):  
John Trinickt ◽  
Howard White
Keyword(s):  
Electron Microscopy ◽  
Atp Hydrolysis ◽  
Myosin Head ◽  
Bound State ◽  
Cross Linking ◽  
Weakly Bound ◽  
Cryo Electron Microscopy ◽  
Myosin Subfragment 1 ◽  
Attached State ◽  
High Fraction

The primary force of muscle contraction is thought to involve a change in the myosin head whilst attached to actin, the energy coming from ATP hydrolysis. This change in attached state could either be a conformational change in the head or an alteration in the binding angle made with actin. A considerable amount is known about one bound state, the so-called strongly attached state, which occurs in the presence of ADP or in the absence of nucleotide. In this state, which probably corresponds to the last attached state of the force-producing cycle, the angle between the long axis myosin head and the actin filament is roughly 45°. Details of other attached states before and during power production have been difficult to obtain because, even at very high protein concentration, the complex is almost completely dissociated by ATP. Electron micrographs of the complex in the presence of ATP have therefore been obtained only after chemically cross-linking myosin subfragment-1 (S1) to actin filaments to prevent dissociation. But it is unclear then whether the variability in attachment angle observed is due merely to the cross-link acting as a hinge.We have recently found low ionic-strength conditions under which, without resorting to cross-linking, a high fraction of S1 is bound to actin during steady state ATP hydrolysis. The structure of this complex is being studied by cryo-electron microscopy of hydrated specimens. Most advantages of frozen specimens over ambient temperature methods such as negative staining have already been documented. These include improved preservation and fixation rates and the ability to observe protein directly rather than a surrounding stain envelope. In the present experiments, hydrated specimens have the additional benefit that it is feasible to use protein concentrations roughly two orders of magnitude higher than in conventional specimens, thereby reducing dissociation of weakly bound complexes.

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