The role of the salt concentration, proton, and phosphate binding on the thermal stability of wild and cloned DNA-binding protein Sso7d from Sulfolobus solfataricus

Todorova, Roumiana; Атанасов, Б.

doi:10.1016/j.ijbiomac.2004.03.013

Cited by 5 publications

(2 citation statements)

References 37 publications

(51 reference statements)

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“…Todorova and Atanasov20 found a stabilizing effect of phosphate on the protein Sso7d of Sulfolobus solfataricus : the denaturation temperature increases in phosphate buffer when compared with that observed in glicin. This could be related to some stabilizing effect of phosphate groups on the protein, in an electrostatic interaction.…”

Section: Resultsmentioning

confidence: 97%

Citrate and phosphate influence on green fluorescent protein thermal stability

Novaes

Mazzola

Pessoa

et al. 2010

Biotechnology Progress

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Protein structure and function can be regulated by no specific interactions, such as ionic interactions in the presence of salts. Green fluorescent protein (GFP) shows remarkable structural stability and high fluorescence; its stability can be directly related to its fluorescence output, among other characteristics. GFP is stable under increasing temperatures, and its thermal denaturation is highly reproducible. The aim of this study was to evaluate the thermal stability of GFP in the presence of different salts at several concentrations and exposed to constant temperatures, in a range of 70-95°C. Thermal stability was expressed in decimal reduction time. It was observed that the D-values obtained were higher in the presence of citrate and phosphate, when compared with that obtained in their absence, indicating that these salts stabilized the protein against thermal denaturation.

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Section: Resultsmentioning

confidence: 97%

Citrate and phosphate influence on green fluorescent protein thermal stability

Novaes

Mazzola

Pessoa

et al. 2010

Biotechnology Progress

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“…Interactions between proteins and other biological molecules, especially nucleic acids, are the foundation of many key biological functions such as transcription, translation, replication, and recombination. , Understanding the protein–DNA interaction has contributed to elucidate mechanisms of protein function and is the central issue of modern molecular biology. , Hyperthermophilic Crenarchaeota has a variety of abundant, sequence-independent DNA-binding proteins, which are able to compact DNA and play a vital role in DNA stabilization at high growth temperatures. − These proteins are characteristic of extreme thermal, acid, and chemical stability as well as DNA binding properties . Such proteins have attracted much interest not only for the academic research but also to the industrial applications. , Many investigators have made great efforts to understand the structure, evolution, hyperthermophilic mechanism, and protein stability. − …”

Section: Introductionmentioning

confidence: 99%

Influence of Hyperthermophilic Protein Cren7 on the Stability and Conformation of DNA: Insights from Molecular Dynamics Simulation and Free Energy Analysis

Chen

Zhang

et al. 2012

J. Phys. Chem. B

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Cren7, a novel chromatin protein highly conserved among crenarchaea, plays an important role in genome packaging and gene regulation. However, the detail dynamical structural characteristic of the Cren7-DNA complex and the detail study of the DNA in the complex have not been done. Focused on two specific Cren7-DNA complexes (PDB codes 3LWH and 3LWI ), we applied molecular dynamics (MD) simulations at four different temperatures (300, 350, 400, and 450 K) and the molecular mechanics Poisson-Boltzmann surface area (MM-PBSA) free energy calculation at 300 and 350 K to examine the role of Cren7 protein in enhancing the stability of DNA duplexes via protein-DNA interactions, and to study the structural transition in DNA. The simulation results indicate that Cren7 stabilizes DNA duplex in a certain temperature range in the binary complex compared with the unbound DNA molecules. At the same time, DNA molecules were found to undergo B-like to A-like form transitions with increased temperature. The results of statistical analyses of the H-bond and hydrophobic contacts show that some residues have significant influence on the structure of DNA molecules. Our work can give important information to understand the interactions of proteins with nucleic acids and other ligands.

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Conformational Changes of Enzymes and DNA in Molecular Dynamics

Chu

Zheng

2013

Dynamics of Proteins and Nucleic Acids

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The role of the salt concentration, proton, and phosphate binding on the thermal stability of wild and cloned DNA-binding protein Sso7d from Sulfolobus solfataricus

Cited by 5 publications

References 37 publications

Citrate and phosphate influence on green fluorescent protein thermal stability

Citrate and phosphate influence on green fluorescent protein thermal stability

Influence of Hyperthermophilic Protein Cren7 on the Stability and Conformation of DNA: Insights from Molecular Dynamics Simulation and Free Energy Analysis

Conformational Changes of Enzymes and DNA in Molecular Dynamics

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