Metal ions provide structural stability and compactness to tetrameric purothionin

RSC Advances ◽  
2016 ◽  
Vol 6 (93) ◽  
pp. 90690-90700 ◽  
Author(s):  
Swagata Das ◽  
Uttam Pal ◽  
Nakul Chandra Maiti
Keyword(s):  
Metal Ions ◽  
Structural Stability

Metal ions impart structural stability to the purothionin tetramer.

scholarly journals Effects of zinc and other metal ions on the stability and activity of Escherichia coli alkaline phosphatase

1971 ◽  
Vol 124 (1) ◽  
pp. 25-30 ◽  
Author(s):  
C. N. A. Trotman ◽  
C. Greenwood
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Metal Ions ◽  
Phosphatase Activity ◽  
Structural Stability ◽  
Zinc Content ◽  
Sedimentation Velocity ◽  
Reducing Agent ◽  
Deficient Mutant ◽  
The Stability

Measurement of the ultraviolet circular dichroism of apo-(alkaline phosphatase) in urea solutions showed substantial denaturation in 3m-urea. A zinc-deficient mutant alkaline phosphatase behaved similarly. The stability of the enzyme in 6m-urea was followed as a function of its zinc content and was found to be dependent on the first two of the four zinc atoms bound by apoenzyme. Phosphatase activity was mostly dependent on a second pair of zinc atoms. Mn2+, Co2+, Cu2+ or Cd2+ also restored structural stability. Sedimentation-velocity and -equilibrium experiments revealed that dissociation of the dimer accompanied apoenzyme denaturation in urea concentrations of 1m or higher, without treatment with disulphide-reducing agent.

Diverse relationships between metal ions and the ribosome

2021 ◽  
Author(s):  
Genki Akanuma
Keyword(s):  
Gene Expression ◽  
Secondary Structure ◽  
Metal Ions ◽  
Structural Stability ◽  
Ribosomal Rna ◽  
Ribosomal Proteins ◽  
Rna Binding ◽  
Cellular Homeostasis ◽  
Ribosomal Subunits ◽  
Translational Activity

Abstract The ribosome requires metal ions for structural stability and translational activity. These metal ions are important for stabilizing the secondary structure of ribosomal RNA, binding of ribosomal proteins to the ribosome, and for interaction of ribosomal subunits. In this review, various relationships between ribosomes and metal ions, especially Mg2+ and Zn2+, are presented. Mg2+ regulates gene expression by modulating the translational stability and synthesis of ribosomes, which in turn contribute to the cellular homeostasis of Mg2+. In addition, Mg2+ can partly complement the function of ribosomal proteins. Conversely, a reduction in the cellular concentration of Zn2+ induces replacement of ribosomal proteins, which mobilizes free-Zn2+ in the cell and represses translation activity. Evolutional relationships between these metal ions and the ribosome are also discussed.

Metal ions in sugar binding, sugar specificity and structural stability of Spatholobus parviflorus seed lectin

2013 ◽  
Vol 19 (8) ◽  
pp. 3271-3278 ◽  
Author(s):  
Joseph Abhilash ◽  
Kalarickal Vijayan Dileep ◽  
Muthusamy Palanimuthu ◽  
Krishnan Geethanandan ◽  
Chittalakkotu Sadasivan ◽  
...  
Keyword(s):  
Metal Ions ◽  
Structural Stability ◽  
Sugar Binding ◽  
Sugar Specificity

scholarly journals Structural stability of the SARS-CoV-2 main protease: Can metal ions affect function?

2020 ◽  
Vol 211 ◽  
pp. 111179 ◽  
Author(s):  
John J. Kozak ◽  
Harry B. Gray ◽  
Roberto A. Garza-López
Keyword(s):  
Metal Ions ◽  
Structural Stability ◽  
Main Protease

Metal ions induced secondary structure rearrangements: mechanically interlocked lassovs.unthreaded branched-cyclic topoisomers

The Analyst ◽  
2018 ◽  
Vol 143 (10) ◽  
pp. 2323-2333 ◽  
Author(s):  
Kevin Jeanne Dit Fouque ◽  
Javier Moreno ◽  
Julian D. Hegemann ◽  
Séverine Zirah ◽  
Sylvie Rebuffat ◽  
...  
Keyword(s):  
Protein Folding ◽  
Secondary Structure ◽  
Metal Ions ◽  
Conformational Change ◽  
Structural Stability ◽  
Significant Role

Metal ions can play a significant role in a variety of important functions in protein systems including cofactor for catalysis, protein folding, assembly, structural stability and conformational change.

HREM Study of electron-induced surface radiation damage in ReO3

1991 ◽  
Vol 49 ◽  
pp. 636-637
Author(s):  
R. Ai ◽  
H.-J. Fan ◽  
L. D. Marks
Keyword(s):  
Transition Metal ◽  
Metal Ions ◽  
Metal Oxides ◽  
Electron Irradiation ◽  
Transition Metal Oxides ◽  
Carbon Film ◽  
Transition Metal Ions ◽  
Surface Radiation ◽  
Valence Transition ◽  
Electron Microscopes

It has been known for a long time that electron irradiation induces damage in maximal valence transition metal oxides such as TiO2, V2O5, and WO3, of which transition metal ions have an empty d-shell. This type of damage is excited by electronic transition and can be explained by the Knoteck-Feibelman mechanism (K-F mechanism). Although the K-F mechanism predicts that no damage should occur in transition metal oxides of which the transition metal ions have a partially filled d-shell, namely submaximal valence transition metal oxides, our recent study on ReO3 shows that submaximal valence transition metal oxides undergo damage during electron irradiation.ReO3 has a nearly cubic structure and contains a single unit in its cell: a = 3.73 Å, and α = 89°34'. TEM specimens were prepared by depositing dry powders onto a holey carbon film supported on a copper grid. Specimens were examined in Hitachi H-9000 and UHV H-9000 electron microscopes both operated at 300 keV accelerating voltage. The electron beam flux was maintained at about 10 A/cm2 during the observation.

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