Identified charged hadron production in collisions at = 200 and 62.4 GeV

Adare, A.*; Afanasiev, S.*; Aidala, C.*; Ajitanand, N. N.*; Akiba, Yasuyuki*; Al-Bataineh, H.*; Alexander, J.*; Aoki, Kazuya*; Aphecetche, L.*; Armendariz, R.*; et al.

Physical Review C, 83(6), p.064903_1 - 064903_29, 2011/06

https://doi.org/10.1103/PhysRevC.83.064903

Transverse momentum distributions and yields for , and in collisions at = 200 and 62.4 GeV at midrapidity are measured by the PHENIX experiment at the RHIC. We present the inverse slope parameter, mean transverse momentum, and yield per unit rapidity at each energy, and compare them to other measurements at different collisions. We also present the scaling properties such as and scaling and discuss the mechanism of the particle production in collisions. The measured spectra are compared to next-to-leading order perturbative QCD calculations.

Measurement of neutral mesons in + collisions at = 200 GeV and scaling properties of hadron production

Adare, A.*; Afanasiev, S.*; Aidala, C.*; Ajitanand, N. N.*; Akiba, Y.*; Al-Bataineh, H.*; Alexander, J.*; Aoki, K.*; Aphecetche, L.*; Armendariz, R.*; et al.

Physical Review D, 83(5), p.052004_1 - 052004_26, 2011/03

https://doi.org/10.1103/PhysRevD.83.052004

The PHENIX experiment at RHIC has measured the invariant differential cross section for production of , , and mesons in collisions at = 200 GeV. The spectral shapes of all hadron transverse momentum distributions are well described by a Tsallis distribution functional form with only two parameters, and , determining the high and characterizing the low regions for the spectra, respectively. The integrated invariant cross sections calculated from the fitted distributions are found to be consistent with existing measurements and with statistical model predictions.

In-plant Measurements of Gamma-ray Transmissions for Precise K-edge and Passive Assay of Plutonium Concentration and Isotopic Fractions in Product Solutions

Russo, P. A.*; Asakura, Yoshiro*; Hsue, S. T.*; Kondo, Isao*; Sprinkle, J. K. Jr.*; Masui, J.*; Johnson, S. S.*; Shoji, J.*

PNC TN841 82-10, 76 Pages, 1982/08

PNC-TN841-82-10.pdf:4.87MB

An instrument based upon high-resolution -ray measurements has beentested for more than 1 year at the TokaiReprocessing Facility for determinationof plutonium concentration by K-edge absorption densitometry and for determination of plutonium isotopic fractions bytransmission-corrected passive -ray spectrometry. The nondestructive assay instrument was designed and built atLos Alamos National Laboratory for theTokai Advanced Safeguards Technology Exercise (TASTEX). It was used at Tokai forthe timely assay of more than 100 productsolution samples daring the TASTEX evaluations The results were compared tosolution samples during the TASTEXaluations. The results were compared toreference values obtained by conventionaldestructive analysis of these samples. The precision and accuracy of plutoniumconcentrations measured by the K-edgetechnique are shown to be with in 0.6% (1) in these applications. The precisionsand accuracies of the isotopic fractions. determined by these passive

None

Miyahara, Kenji; Asakura, Yoshiro*; *; Masui, J.*; Kondo, Isao*; *; Kamata, Masayuki; *

PNC TN852 81-15, 46 Pages, 1981/04

PNC-TN852-81-15.pdf:2.23MB

None

None

Tsuboya, Takao*; Kamata, Masayuki; Wada, Yukio; Masui, J.*; *; Wada, Tsutomu*; ; *

PNC TN851 76-01, 42 Pages, 1976/01

PNC-TN851-76-01.pdf:1.26MB

None

The Structure formation of filamentous actin and polycation complex

Masui, Tomomi; Shikinaka, Kazuhiro*; Kwon, H.*; Koizumi, Satoshi; Hashimoto, Takeji; Iwase, Hiroki; Kakugo, Akira*; Gong, J.*

no journal, , 

no abstracts in English

In situ observation on hierarchical actin bundle network

Masui, Tomomi; Shikinaka, Kazuhiro*; Kwon, H.*; Koizumi, Satoshi; Hashimoto, Takeji; Iwase, Hiroki; Kakugo, Akira*; Gong, J.*

no journal, , 

Actin is one of the most abundant cytoskeleton proteins in eucaryotic cell. They play a crucialrole in cell motility by polymerizing monomeric globular G-actin into polymeric filamentous actin (F-actin). With actin-binding proteins (ABPs), they form higher order structures such as linear bundles, two-dimensional networks and three-dimensional gels. It has been considered that these structures are controlled by ABPs. However recent study have shown that the only one kind of artificial cationic polymer can form variety of structures depending its concentration and salt concentration. This system is a good model to elucidate the mechanism of regulation of actin and ABPs complex structure. Based on these backgrounds, we have investigated the effects of salt concentration on the stability and structure of actin-polycation complexes by using small angle neutron scattering (SANS) technique.

In situ observation on hierarchical actin bundle networks; Salt concentration effects

Masui, Tomomi; Shikinaka, Kazuhiro*; Kwon, H.*; Koizumi, Satoshi; Hashimoto, Takeji; Iwase, Hiroki; Kakugo, Akira*; Gong, J.*

no journal, , 

Actin is one of the cytoskeleton proteins and it is most abundant proteins in eucaryotic cell. They play a crucial role in cell motility by polymerization of monomeric globular G-actin into polymeric filamentous actin (F-actin). With actin binding proteins, they form various structures such as linear bundles, two-dimensional networks, and three-dimensional gels. It has been considered that these structures are controlled by the specific interaction between actin and binding protein. However from the physicochemical point of view, actin has negative charge and actin-binding protein has positive charge. Thus, the electrostatic interaction might play important role to determinein the structure. Based on this idea, we have investigated the effects of salt concentration on the stability and structure of actin-polymer complexes by using small angle neutron scattering (SANS) technique.

Assembly and disassembly of model cytoskeleton system

Masui, Tomomi; Shikinaka, Kazuhiro*; Kwon, H.*; Koizumi, Satoshi; Hashimoto, Takeji; Iwase, Hiroki; Kakugo, Akira*; Gong, J.*

no journal, , 

Actin is one of the most abundant cytoskeleton proteins in eucaryotic cell. They play a crucial role in cell motility by polymerizing monomeric globular G-actin into polymeric filamentous actin (F-actin). Withactin-binding proteins (ABPs), they form higher order structures such as linear bundles, two-dimensional networks and three-dimensional gels. In this study we have constructed model cytoskeleton system composed of F-actin, cationic polymer and salt. To investigate salt induced hierarchical structure change we employed fluorescence microscopy and small angle neutron scattering (SANS) technique.

Salt induced hierarchical morphology change of actin/polycation complexes

Masui, Tomomi; Shikinaka, Kazuhiro*; Koizumi, Satoshi; Kakugo, Akira*; Hashimoto, Takeji; Gong, J.*

no journal, , 

Hierarchical structures of F-actin, an anionic polyelectrolyte, and PDMAPAA-Q, a synthetic linear cationic polyelectrolyte (polycation), complexes in KCl salt solutions have been examined over a wide range of length scales from nanometer to micrometer using a combination of ultra-small-angle neutron scattering technique and fluorescence microscopy. We found hierarchical condensation of actin/polycation complex composed of a superbundle of 10 micrometer, protobundle of 100 nanometer, and protofilament (F-actin) of nanometer. These structures are largely influenced by salt concentrations. With increase of salt concentration superbundle structure changes from globular to extended states, simultaneously, the regularity of F-actin inside the protobundle increased and protobundle size increased about ten times larger. Further increase of salt concentration brings the protobundle disassemble to single F-actin.