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>
Answer:
IV
Explanation:
The complete question is shown in the image attached.
Let us call to mind the fact that the SN1 mechanism involves the formation of carbocation in the rate determining step. The order of stability of cabocations is; tertiary > secondary > primary > methyl.
Hence, a tertiary alkyl halide is more likely to undergo nucleophilic substitution reaction by SN1 mechanism since it forms a more stable cabocation in the rate determining step.
Structure IV is a tertiary alkyl halide, hence it is more likely to undergo nucleophilic substitution reaction by SN1 mechanism.
This is false. One mole of a gas occupies 22.4 L at STP, which is taken to be 0°C (273 K) and 1 atm. If atmospheric conditions depart from these values, this assumption cannot be used.
