Answer:
Copper(II) sulphate – sodium hydroxide reaction
The reaction between copper(Il) sulphate and sodium hydroxide solutions is a good place to start. If you slowly add one to the other while stirring, you will get a precipitate of copper(II) hydroxide, Cu(OH)2.
Answer:
E = 1.602v
Explanation:
Use the Nernst Equation => E(non-std) = E⁰(std) – (0.0592/n)logQc …
Zn⁰(s) => Zn⁺²(aq) + 2 eˉ
2Ag⁺(aq) + 2eˉ=> 2Ag⁰(s)
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Zn⁰(s) + 2Ag⁺(aq) => Zn⁺²(aq) + 2Ag(s)
Given E⁰ = 1.562v
Qc = [Zn⁺²(aq)]/[Ag⁺]² = (1 x 10ˉ³)/(0.150)² = 0.044
E = E⁰ -(0.0592/n)logQc = 1.562v – (0.0592/2)log(0.044) = 1.602v
Answer: Each pair of shared electrons is a covalent bond which can be represented by a dash.
Explanation:
In a Lewis dot structure, the central atom can share electrons through bonds with the surrounding atoms, and this can look like a dash between the atoms.
Answer:
physical change because even though gas formation was observed the water was undergoing a state change which means that it's original properties are preserved
Answer:
The answer is IONIC BOND
Explanation:
Steroidogenic acute regulatory, (StAR) protein is a type of globular protein, which allows it act as an active catalyst on substrates. Because the substrates on which enzymes act usually have higher molecular weights of several hundred as compared to the enzymes, only a fraction of the enzyme's surface is in contact with the substrate. This region of contact called the <em>active site</em>, is as a result of the protein folding itself into a tertiary structure.
Once the correct substrate has bound at the active site of the enzyme, an enzyme-substrate complex is created. The substrate is usually held in the complex by combinations of electrical attraction, hydrophobic repulsion, or hydrogen bonding between and from the amino acid; the strongest of which is the ionic/electrostatic bonding due to larger amount of ionic "R" groups in the protein structure.
So whilst all these inter-molecular interactions are possible, the strongest would be <u>ionic bond.</u>