C) H2O has the strongest dipole interactions
Explanation:
The dipole interactions are the interactions that occur between polar molecules.
Polar molecules form when the atoms forming the molecule have different electronegativity, therefore one of the atom in the molecule attract the shared electrons more towards itself; as a result, the molecule ends up having a region which is slightly negatively charged and a region slightly positively charged.
In this problem, we are comparing 4 different molecules. We observe that:
H2: this molecule is formed by 2 atoms of hydrogen - since the two atoms are identical, electrons are equally shared between the two atoms, so this molecule is not polar
O2: this molecule is formed by 2 identical atoms of oxygen, so it is not polar, for the same reason as H2
CH4: this molecule consists of a carbon atom surrounded by 4 hydrogen atoms - since this molecule has a symmetric structure, the charge is balanced, therefore this molecule is not polar
H2O (water): the oxygen atom in the water molecule is more electronegative than the hydrogens, therefore it tends to attract more the shared electrons - as a result, the molecule is polar.
Therefore, the correct answer is H2O.
Learn more about atoms and molecules:
brainly.com/question/2757829
#LearnwithBrainly
The sun does not orbit around any plants
Answer:
from equation 4.9 v = at = 9.8 m/s2 * 2 s =20 m/s.
Explanation:
Answer:
The lock-and-key model:
c. Enzyme active site has a rigid structure complementary
The induced-fit model:
a. Enzyme conformation changes when it binds the substrate so the active site fits the substrate.
Common to both The lock-and-key model and The induced-fit model:
b. Substrate binds to the enzyme at the active site, forming an enzyme-substrate complex.
d. Substrate binds to the enzyme through non-covalent interactions
Explanation:
Generally, the catalytic power of enzymes are due to transient covalent bonds formed between an enzyme's catalytic functional group and a substrate as well as non-covalent interactions between substrate and enzyme which lowers the activation energy of the reaction. This applies to both the lock-and-key model as well as induced-fit mode of enzyme catalysis.
The lock and key model of enzyme catalysis and specificity proposes that enzymes are structurally complementary to their substrates such that they fit like a lock and key. This complementary nature of the enzyme and its substrates ensures that only a substrate that is complementary to the enzyme's active site can bind to it for catalysis to proceed. this is known as the specificity of an enzyme to a particular substrate.
The induced-fit mode proposes that binding of substrate to the active site of an enzyme induces conformational changes in the enzyme which better positions various functional groups on the enzyme into the proper position to catalyse the reaction.