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 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’.

Microstructure and thermal stability of amorphous materials in the GeS2−La2S3 system

1991 ◽  
Vol 6 (12) ◽  
pp. 2694-2700 ◽  
Author(s):  
Prashant N. Kumta ◽  
Subhash H. Risbud
Keyword(s):  
Thermal Stability ◽  
Amorphous Materials ◽  
Fiber Optic ◽  
Molecular Level ◽  
Infrared Region ◽  
Mid Infrared ◽  
Heat Treated ◽  
Stable Glasses ◽  
Microstructural Studies ◽  
Thermal Stability Of

GeS2 is known to be a good chalcogenide glass former with a transmission cutoff at 11 μm and has been studied for fiber optic application in the mid infrared region. The rare earth sulfides, oxysulfides, and oxides (La–Er) form reasonably good and stable glasses when mixed with chalcogenides such as Ga2S3. In this work, glass formation was studied in the GeS2−La2S3 system. Two compositions containing 60 mol % and 92.5 mol % GeS2, respectively, were analyzed, and the effects of composition on the microstructure and thermal stability of these glasses were investigated. Microstructural studies were conducted on the as-prepared and heat-treated glasses using TEM and SEM/EDXA. Glasses rich in GeS2 exhibited primary (6–88 nm) and secondary (3–13 nm) phase separation at the molecular level. Differential thermal analysis performed on these glasses indicated glass transition temperatures (Tg) of 510 °C and 420 °C for the two compositions studied. The glasses were stable and the (Tg) was observed to decrease with increasing contents of GeS2 in these glasses.

Multi-scale thermal stability of niobate-based lead-free piezoceramics with large piezoelectricity

2015 ◽  
Vol 3 (34) ◽  
pp. 8780-8787 ◽  
Author(s):  
Jin-Song Zhou ◽  
Ke Wang ◽  
Fang-Zhou Yao ◽  
Ting Zheng ◽  
Jiagang Wu ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Lead Free ◽  
Multi Scale ◽  
Thermal Stability Of

Multi-scale thermal stability of (K,Na)NbO3-based perovskites with a high d33 of 430 pC N−1 is investigated, revealing the origin of its large piezoelectricity.

scholarly journals Phase transition and thermal stability of epitaxial PtSe2 nanolayer on Pt(111)

RSC Advances ◽  
2020 ◽  
Vol 10 (51) ◽  
pp. 30934-30943 ◽  
Author(s):  
Yongfeng Tong ◽  
Meryem Bouaziz ◽  
Hamid Oughaddou ◽  
Hanna Enriquez ◽  
Karine Chaouchi ◽  
...  
Keyword(s):  
Phase Transition ◽  
Thermal Stability ◽  
Chemical Deposition ◽  
Deposition Method ◽  
Temperature Dependent ◽  
Chemical Deposition Method ◽  
Thermal Stability Of

LEED, STM and XPS techniques were used to systematically study a temperature-dependent phase transition on a PtSe2 film grown on the surface of Pt(111) by a chemical deposition method.

scholarly journals Engineering Improves Enzymatic Synthesis of L-Tryptophan by Tryptophan Synthase from Escherichia coli

2020 ◽  
Vol 8 (4) ◽  
pp. 519
Author(s):  
Lisheng Xu ◽  
Fangkai Han ◽  
Zeng Dong ◽  
Zhaojun Wei
Keyword(s):  
Thermal Stability ◽  
Amino Acid ◽  
Directed Evolution ◽  
Amino Acid Residue ◽  
Rational Design ◽  
Molecular Engineering ◽  
Mutant Enzyme ◽  
Tryptophan Synthase ◽  
Mutant Library ◽  
Thermal Stability Of

To improve the thermostability of tryptophan synthase, the molecular modification of tryptophan synthase was carried out by rational molecular engineering. First, B-FITTER software was used to analyze the temperature factor (B-factor) of each amino acid residue in the crystal structure of tryptophan synthase. A key amino acid residue, G395, which adversely affected the thermal stability of the enzyme, was identified, and then, a mutant library was constructed by site-specific saturation mutation. A mutant (G395S) enzyme with significantly improved thermal stability was screened from the saturated mutant library. Error-prone PCR was used to conduct a directed evolution of the mutant enzyme (G395S). Compared with the parent, the mutant enzyme (G395S /A191T) had a Km of 0.21 mM and a catalytic efficiency kcat/Km of 5.38 mM−1∙s−1, which was 4.8 times higher than that of the wild-type strain. The conditions for L-tryptophan synthesis by the mutated enzyme were a L-serine concentration of 50 mmol/L, a reaction temperature of 40 °C, pH of 8, a reaction time of 12 h, and an L-tryptophan yield of 81%. The thermal stability of the enzyme can be improved by using an appropriate rational design strategy to modify the correct site. The catalytic activity of tryptophan synthase was increased by directed evolution.

Correlating disease-related mutations to their effect on protein stability: A large-scale analysis of the human proteome

2011 ◽  
Vol 32 (10) ◽  
pp. 1161-1170 ◽  
Author(s):  
Rita Casadio ◽  
Marco Vassura ◽  
Shalinee Tiwari ◽  
Piero Fariselli ◽  
Pier Luigi Martelli
Keyword(s):  
Protein Stability ◽  
Large Scale ◽  
Human Proteome ◽  
Scale Analysis ◽  
Large Scale Analysis
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