scholarly journals Thermal stability of lysozyme as a function of ion concentration: A reappraisal of the relationship between the Hofmeister series and protein stability

2013 ◽  
Vol 22 (11) ◽  
pp. 1563-1570 ◽  
Author(s):  
Jordan W. Bye ◽  
Robert J. Falconer
Keyword(s):  
Thermal Stability ◽  
Protein Stability ◽  
Ion Concentration ◽  
Hofmeister Series ◽  
The Relationship ◽  
Thermal Stability Of

Thermal stability of ribosomes from a thermophilic and a mesophilic fungus

1973 ◽  
Vol 19 (6) ◽  
pp. 761-763 ◽  
Author(s):  
H. M. Miller ◽  
M. G. Shepherd
Keyword(s):  
Thermal Stability ◽  
Ion Concentration ◽  
Magnesium Ion ◽  
Penicillium Notatum ◽  
Ribosomal Subunits ◽  
Ion Concentrations ◽  
Thermal Stability Of

Ribosomes and ribosomal subunits from the thermophile Penicillium duponti were found to be more thermostable than the corresponding particles from the mesophile Penicillium notatum. The thermostability of the ribosomes from both organisms was dependent on magnesium ion concentration. The dissociation of the 80-S ribosomes into 60-S and 40-S subunits occurred at higher magnesium ion concentrations for the mesophile than the thermophile.

scholarly journals Investigation of the Relationship between the Residual Moisture and Thermal Stability of Lyophilized MMR Vaccine

2009 ◽  
Vol 3 (1) ◽  
pp. 25-28 ◽  
Author(s):  
MK Shahkarami ◽  
M Taqavian ◽  
A Shafyi ◽  
B Alirezaie ◽  
F Esna-ashari ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Mmr Vaccine ◽  
Residual Moisture ◽  
The Relationship ◽  
Thermal Stability Of

scholarly journals Improved Insights into Protein Thermal Stability: From the Molecular to the Structurome Scale

2016 ◽  
Author(s):  
Fabrizio Pucci ◽  
Marianne Rooman
Keyword(s):  
Thermal Stability ◽  
Amino Acid ◽  
Protein Stability ◽  
Large Scale ◽  
Molecular Level ◽  
Temperature Dependent ◽  
Natural Evolution ◽  
Multi Scale ◽  
Large Scale Analysis ◽  
Thermal Stability Of

AbstractDespite the intense efforts of the last decades to understand the thermal stability of proteins, the mechanisms responsible for its modulation still remain debated. In this investigation, we tackle this issue by showing how a multi-scale perspective can yield new insights. With the help of temperature-dependent statistical potentials, we analyzed some amino acid interactions at the molecular level, which are suggested to be relevant for the enhancement of thermal resistance. We then investigated the thermal stability at the protein level by quantifying its modification upon amino acid substitutions. Finally, a large scale analysis of protein stability - at the structurome level - contributed to the clarification of the relation between stability and natural evolution, thereby showing that the mutational profile of thermostable and mesostable proteins differ. Some final considerations on how the multi-scale approach could help unraveling the protein stability mechanisms are briefly discussed.

scholarly journals Fuel Deposit Characteristics at Low Velocity

1985 ◽  
Author(s):  
E. J. Szetela ◽  
A. J. Giovanetti ◽  
S. Cohen
Keyword(s):  
Thermal Stability ◽  
Operating Time ◽  
Test Tube ◽  
Experimental Program ◽  
Fuel System ◽  
Low Velocity ◽  
Steel Tubes ◽  
The Relationship ◽  
Thermal Stability Of

An experimental program has been carried out to characterize the relationship between deposit mass, operating time and temperature in studies of the thermal stability of aviation gas turbine fuel. This information is required by fuel system designers to prevent deposit build-up in fuel system components, thus allowing for more efficient designs. The program has included the design, fabrication, and operation of a novel thermal stability test apparatus for the determination of deposition rates over a range of temperatures and test durations up to several hundred hours. Experiments were run to determine the rate of deposit formation as a function of temperature in heated stainless steel tubes at low velocity using Jet A fuel. The test tube had an inside diameter of 0.22 cm, a length of 0.91 m, and a flow rate of 0.73 kg/hr. Deposits obtained were often characterized as thick, porous, and non-uniform in nature. Deposit density, based on carbon content was 0.08 g/cm3. Deposit rates of 0.1 to 100 μgC/hr-cm2 were observed at surface temperatures between 400 and 600 K.

scholarly journals Improved insights into protein thermal stability: from the molecular to the structurome scale

2016 ◽  
Vol 374 (2080) ◽  
pp. 20160141 ◽  
Author(s):  
Fabrizio Pucci ◽  
Marianne Rooman
Keyword(s):  
Thermal Stability ◽  
Amino Acid ◽  
Protein Stability ◽  
Large Scale ◽  
Molecular Level ◽  
Multiscale Approach ◽  
Temperature Dependent ◽  
Natural Evolution ◽  
Large Scale Analysis ◽  
Thermal Stability Of

Despite the intense efforts of the last decades to understand the thermal stability of proteins, the mechanisms responsible for its modulation still remain debated. In this investigation, we tackle this issue by showing how a multiscale perspective can yield new insights. With the help of temperature-dependent statistical potentials, we analysed some amino acid interactions at the molecular level, which are suggested to be relevant for the enhancement of thermal resistance. We then investigated the thermal stability at the protein level by quantifying its modification upon amino acid substitutions. Finally, a large scale analysis of protein stability—at the structurome level—contributed to the clarification of the relation between stability and natural evolution, thereby showing that the mutational profile of proteins differs according to their thermal properties. Some considerations on how the multiscale approach could help in unravelling the protein stability mechanisms are briefly discussed. This article is part of the themed issue ‘Multiscale modelling at the physics–chemistry–biology interface’.

scholarly journals Effect of Lanthanum Doping on the Microstructure, Thermal Stability, and CO2 Adsorption Property of ZIF-8

2019 ◽  
Vol 2019 ◽  
pp. 1-7 ◽  
Author(s):  
Sheng Wang ◽  
Shengquan Zhang ◽  
Xueyan Du ◽  
Yingying Shen ◽  
Zhiwei Ma
Keyword(s):  
Thermal Stability ◽  
Adsorption Property ◽  
Research Process ◽  
X Ray Diffraction ◽  
Lanthanum Doping ◽  
Microstructure Stability ◽  
Structure Morphology ◽  
Metal Organic ◽  
The Relationship ◽  
Thermal Stability Of

The reaction materials La(NO3)3·6H2O, Zn(NO3)2·6H2O, and 2-methylimidazole were mixed in a certain proportion. A research process innovatively adopts the parallel flow-drop solvothermal method and a lanthanum-doping method to achieve the synthesis of metal organic frameworks. In this study, we successfully introduce lanthanum into the framework of ZIF-8 to stabilize the spatial structure and improve its performance. The structure and properties of La-ZIF-8 were characterized by the X-ray diffraction (XRD), scanning electron microscope (SEM), thermogravimetry analysis (TGA), and fourier transform infrared spectroscopy (FTIR). The relationship between microstructure stability and macroscopical properties is illustrated. The results show that the doping of lanthanum is beneficial for improving the thermal stability and CO2 adsorption property of ZIF-8 because of the improvement in the microstructure. The introduction of lanthanum to the ZIF-8 is also beneficial for forming porous frameworks and raising the thermal stability and CO2 adsorption properties. The crystallinity, structure, morphology, and thermal stability of La-ZIF-8 are optimal at the La content of 2 atom.%.

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