An Experimental Approach to the Determination of Comparative Efficiency of Insulin and Convulsion Therapy

1943 ◽  
Vol 98 (6) ◽  
pp. 666
Author(s):  
H. A. Palmer
Keyword(s):  
Experimental Approach ◽  
Comparative Efficiency

Experimental Determination of the Effective Resolution Limit in Thick Specimens at High Voltages

1975 ◽  
Vol 33 ◽  
pp. 664-665
Author(s):  
Mircea Fotino
Keyword(s):  
Experimental Approach ◽  
Chromatic Aberration ◽  
Resolving Power ◽  
Biological Research ◽  
Specimen Thickness ◽  
Resolution Limit ◽  
High Voltage Electron Microscopy ◽  
Voltage Electron ◽  
Resolution Level

The use of thick specimens (0.5 μm to 5.0 μm or more) is one of the most resourceful applications of high-voltage electron microscopy in biological research. However, the energy loss experienced by the electron beam in the specimen results in chromatic aberration and thus in a deterioration of the effective resolving power. This sets a limit to the maximum usable specimen thickness when investigating structures requiring a certain resolution level.An experimental approach is here described in which the deterioration of the resolving power as a function of specimen thickness is determined. In a manner similar to the Rayleigh criterion in which two image points are considered resolved at the resolution limit when their profiles overlap such that the minimum of one coincides with the maximum of the other, the resolution attainable in thick sections can be measured by the distance from minimum to maximum (or, equivalently, from 10% to 90% maximum) of the broadened profile of a well-defined step-like object placed on the specimen.

Reynolds-averaged Navier–Stokes simulation of hydrofoil effects on hydrodynamic coefficients of a catamaran in forced oscillation

2016 ◽  
Vol 231 (2) ◽  
pp. 364-383
Author(s):  
Amin Najafi ◽  
Mohammad Saeed Seif
Keyword(s):  
High Speed ◽  
Experimental Approach ◽  
Navier Stokes ◽  
Hydrodynamic Coefficients ◽  
Laboratory Equipment ◽  
Factors Affecting ◽  
High Frequencies ◽  
Frequency Independent ◽  
Reynolds Averaged Navier Stokes

Determination of high-speed crafts’ hydrodynamic coefficients will help to analyze the dynamics of these kinds of vessels and the factors affecting their dynamic stabilities. Also, it can be useful and effective in controlling the vessel instabilities. The main purpose of this study is to determine the coefficients of longitudinal motions of a planing catamaran with and without a hydrofoil using Reynolds-averaged Navier–Stokes method to evaluate the foil effects on them. Determination of hydrodynamic coefficients by experimental approach is costly and requires meticulous laboratory equipment; therefore, utilizing the numerical methods and developing a virtual laboratory seem highly efficient. In this study, the numerical results for hydrodynamic coefficients of a high-speed craft are verified against Troesch’s experimental results. In the following, after determination of hydrodynamic coefficients of a planing catamaran with and without foil, the foil effects on its hydrodynamic coefficients are evaluated. The results indicate that most of the coefficients are frequency-independent especially at high frequencies.

NMR for the design of functional mimetics of protein-protein interactions: one key is in the building of bridges

1998 ◽  
Vol 76 (2-3) ◽  
pp. 177-188 ◽  
Author(s):  
Jianxing Song ◽  
Feng Ni
Keyword(s):  
Protein Interactions ◽  
Binding Sites ◽  
Experimental Approach ◽  
Structural Information ◽  
Peptide Ligands ◽  
Protein Protein Interactions ◽  
Binding Residues ◽  
Related Proteins ◽  
Binding Inhibitors

Using the design of bivalent and bridge-binding inhibitors of thrombin as an example, we review an NMR-based experimental approach for the design of functional mimetics of protein-protein interactions. The strategy includes: (i) identification of binding residues in peptide ligands by differential resonance perturbation, (ii) determination of protein-bound structures of peptide ligands by use of transferred NOEs, (iii) minimization of larger protein and peptide ligands on the basis of NMR structural information, and (iv) linkage of two weakly binding mimetics to produce an inhibitor with enhanced affinity and specificity. This approach can be especially effective for the design of potent and selective functional mimetics of protein-protein interactions because it is less likely that the surfaces of two related proteins or enzymes share two identical binding sites or regions.Key words: NMR, protein-protein interactions, functional mimetics, bridge-binding inhibitors, thrombin.

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