scholarly journals Shape-coexistence Studies in the Ni Isotopic Chain by Using the Selectivity of Different Reaction Mechanisms

2020 ◽  
Vol 51 (3) ◽  
pp. 807
Author(s):  
S. Leoni ◽  
B. Fornal ◽  
N. Marginean ◽  
C. Michelagnoli ◽  
J. Wilson ◽  
...  
2019 ◽  
Vol 223 ◽  
pp. 01072
Author(s):  
Irene Zanon ◽  
Marco Siciliano ◽  
Alain Goasduff ◽  
Philipp R. John

The mercury isotopic chain is depicted as one of the best fields to observe many phenomena related to collectivity evolution as, for instance, shape transition, shape coexistence or shape staggering. In this context, the 189Hg presents several interesting aspects and is still relatively unexplored. The nucleus has been studied at the Laboratori Nazionali di Legnaro using a fusion-evaporation reaction and the γ rays emitted have been detected by the GALILEO array, coupled with Neutron Wall and the GALILEO plunger. The presorting and the preliminary results are presented.


2019 ◽  
Vol 50 (3) ◽  
pp. 605 ◽  
Author(s):  
S. Leoni ◽  
B. Fornal ◽  
N. Marginean ◽  
M. Sferrazza ◽  
Y. Tsunoda ◽  
...  

2019 ◽  
Vol 28 (10) ◽  
pp. 1950086
Author(s):  
S. Shohani ◽  
A. Kardan

The Po isotopes show the presence of coexisting structures having different deformations with increasing neutron number within the macroscopic–microscopic Nilsson–Strutinsky formalism. The model is based on the Lublin Strasbourg Drop (LSD) method for the macroscopic energy calculation. We study the shape evolution in a long chain of polonium isotopes, [Formula: see text]Po.


Author(s):  
Jeff Gelles

Mechanoenzymes are enzymes which use a chemical reaction to power directed movement along biological polymer. Such enzymes include the cytoskeletal motors (e.g., myosins, dyneins, and kinesins) as well as nucleic acid polymerases and helicases. A single catalytic turnover of a mechanoenzyme moves the enzyme molecule along the polymer a distance on the order of 10−9 m We have developed light microscope and digital image processing methods to detect and measure nanometer-scale motions driven by single mechanoenzyme molecules. These techniques enable one to monitor the occurrence of single reaction steps and to measure the lifetimes of reaction intermediates in individual enzyme molecules. This information can be used to elucidate reaction mechanisms and determine microscopic rate constants. Such an approach circumvents difficulties encountered in the use of traditional transient-state kinetics techniques to examine mechanoenzyme reaction mechanisms.


Author(s):  
A. Angel ◽  
K. Miller ◽  
V. Seybold ◽  
R. Kriebel

Localization of specific substances at the ultrastructural level is dependent on the introduction of chemicals which will complex and impart an electron density at specific reaction sites. Peroxidase-antiperoxidase(PAP) methods have been successfully applied at the electron microscopic level. The PAP complex is localized by addition of its substrate, hydrogen peroxide and an electron donor, usually diaminobenzidine(DAB). On oxidation, DAB forms an insoluble polymer which is able to chelate with osmium tetroxide becoming electron dense. Since verification of reactivity is visual, discrimination of reaction product from osmiophillic structures may be difficult. Recently, x-ray microanalysis has been applied to examine cytochemical reaction precipitates, their distribution in tissues, and to study cytochemical reaction mechanisms. For example, immunoreactive sites labelled with gold have been ascertained by means of x-ray microanalysis.


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