scholarly journals DETERMINATION OF THE OPTIMUM TIME OF REPLACEMENT OF THE VEHICLE

2021 ◽  
Vol 1 (1) ◽  
pp. 193-194
Author(s):  
Yuliya Poltavskaya
Keyword(s):  
Life Cycle ◽  
Economic Analysis ◽  
Optimum Time ◽  
Optimal Period

A method for determining the optimal period of vehicle replacement based on the economic analysis of the life cycle is considered

Quantifying Office Productivity: An Ergonomic Framework

1998 ◽  
Vol 42 (13) ◽  
pp. 974-978 ◽  
Author(s):  
Alan Hedge
Keyword(s):  
Life Cycle ◽  
Duty Cycle ◽  
Office Workers ◽  
Short Term ◽  
Task Time ◽  
Ergonomic Interventions ◽  
The Impact

An ergonomic framework for conceptualizing and measuring office productivity is described. This framework is based on the the analysis of task time, posture and sequence, and the subsequent the determination of the most appropriate pace, posture, and activities for any office job. The framework assesses various measures of pace, proficiency, and posture that currently can be readily assessed by ergonomists, and it uses these measures to quantify the short-term duty cycle productivity (DCP) and in the longer-term life-cycle productivity (LCP) of office workers. The approach that will be described allows companies to evaluate the impact of ergonomic interventions on the productivity of their workers. The benefits of this ergonomic approach to assessing productivity are discussed.

scholarly journals Structural, functional and computational studies of membrane recognition by Plasmodium Perforin-Like Proteins 1 and 2.

2021 ◽  
Author(s):  
Sophie Williams ◽  
Xiulian Yu ◽  
Tao Ni ◽  
Robert Gilbert ◽  
Phillip Stansfeld
Keyword(s):  
Life Cycle ◽  
Lipid Bilayers ◽  
Membrane Binding ◽  
Binding Activity ◽  
Life Cycles ◽  
Site Directed Mutagenesis ◽  
Parasite Life Cycle ◽  
Dynamics Simulations ◽  
Membrane Recognition

Perforin-like proteins (PLPs) play key roles in the mechanisms associated with parasitic disease caused by apicomplexans such as Plasmodium (malaria) and Toxoplasma. The T. gondii PLP1 (TgPLP1) mediates tachyzoite egress from cells, while the five Plasmodium PLPs carry out various roles in the life cycle of the parasite and with respect to the molecular basis of disease. Here we focus on Plasmodium vivax PLP1 and PLP2 (PvPLP1 and PvPLP2) compared to TgPLP1; PvPLP1 is important for invasion of mammalian hosts by the parasite and establishment of a chronic infection, PvPLP2 is important during the symptomatic blood stage of the parasite life cycle. Determination of the crystal structure of the membrane-binding APCβ domain of PvPLP1 reveals notable differences with that of TgPLP1, which are reflected in its inability to bind lipid bilayers in the way that TgPLP1 and PvPLP2 can be shown to. Molecular dynamics simulations combined with site-directed mutagenesis and functional assays allow a dissection of the binding interactions of TgPLP1 and PvPLP2 on lipid bilayers, and reveal a similar tropism for lipids found enriched in the inner leaflet of the mammalian plasma membrane. In addition to this shared mode of membrane binding PvPLP2 displays a secondary synergistic interaction side-on from its principal bilayer interface. This study underlines the substantial differences between the biophysical properties of the APCβ domains of Apicomplexan PLPs, which reflect their significant sequence diversity. Such differences will be important factors in determining the cell targeting and membrane-binding activity of the different proteins, in their different developmental roles within parasite life cycles.

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