scholarly journals An Independent Determination of the Binding Energy of the Deuteron

1939 ◽  
Vol 55 (3) ◽  
pp. 263-269 ◽  
Author(s):  
F. T. Rogers ◽  
Marguerite M. Rogers

2021 ◽  
Vol 126 (9) ◽  
Author(s):  
M. Ablikim ◽  
M. N. Achasov ◽  
P. Adlarson ◽  
S. Ahmed ◽  
M. Albrecht ◽  
...  


1954 ◽  
Vol 207 (2) ◽  
pp. 903-910
Author(s):  
R.D. Strickland ◽  
E.L. Martin ◽  
J.L. Riebsomer


Leaving out of consideration those nuclei of small atomic number it is possible to develop a statistical theory of nuclei. Bethe and Bacher (1936, p. 149), as well as many other writers, have treated this subject in great detail starting from the Hartree approximation. All these investigations were mainly concerned with the binding energy, and not much attention has been paid so far to the stability of nuclei according to the statistical theory, except the determination of the most stable nucleus with a given atomic number: this is due to the fact that previous investigators have always neglected to distinguish between quantum states with opposite spin, thereby losing the distinction between “odd” and “even” nuclei, which is essential for stability considerations.



Triose phosphate isomerase is a dimeric enzyme of molecular mass 56000 which catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate. The crystal structure of the enzyme from chicken muscle has been determined at a resolution of 2.5 A, and an independent determination of the structure of the yeast enzyme has just been completed at 3 A resolution. The conformation of the polypeptide chain is essentially identical in the two structures, and consists of an inner cylinder of eight strands of parallel |3-pleated sheet, with mostly helical segments connecting each strand. The active site is a pocket containing glutamic acid 165, which is believed to act as a base in the reaction. Crystallographic studies of the binding of DHAP to both the chicken and the yeast enzymes reveal a common mode of binding and suggest a mechanism for catalysis involving polarization of the substrate carbonyl group.



1988 ◽  
Vol 206 (2) ◽  
pp. 187-189 ◽  
Author(s):  
E.L. Tomusiak ◽  
H. Arenhövel


2017 ◽  
Author(s):  
Saúl González-Lemos ◽  
José Guitián ◽  
Miguel-Ángel Fuertes ◽  
José-Abel Flores ◽  
Heather M. Stoll

Abstract. As major calcifiers in the open ocean, coccolithophores play a key role in the marine carbon cycle. Because they may be sensitive to changing CO2 and ocean acidification, there is significant interest in quantifying past and present variations in their cellular calcification by quantifying the thickness of the coccoliths or calcite plates that cover their cells. Polarized light microscopy has emerged as a key tool for quantifying the thickness of these calcite plates, but the reproducibility and accuracy of such determinations has been limited by the absence of suitable calibration materials in the thickness range of coccoliths (0–4 microns). Here, we describe the fabrication of a calcite wedge with a constant slope over 15 this thickness range, and the independent determination of calcite thickness along the wedge profile. We show how the calcite wedge provides more robust calibrations in the 0 to 1.55 μm range than previous approaches using rhabdoliths. We show the particular advantages of the calcite wedge approach for developing equations to relate thickness to the interference colors that arise in calcite in the thickness range between 1.55 and 4 μm. The calcite wedge approach can be applied to develop equations relevant to the particular light spectra and intensity of any polarized light microscope system and could significantly improve within and inter-laboratory data comparability.



2015 ◽  
Vol 51 (81) ◽  
pp. 15071-15074 ◽  
Author(s):  
Bora Joo ◽  
Eung-Gun Kim

Choosing a small active space of electrons for charge analysis allows the model-free determination of the degree of charge transfer.



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