The volume<span> of </span>gas<span> because of the </span>increase<span> and decrease in the speed in which the molecules bounce around. ... Boyle's Law states that if temperature stays the same, the </span>amount of<span> space a </span>gas takes up will increase<span> if the </span>pressure<span> decreases. The </span>amount of gas<span> will take up less space if the </span>pressure<span> is increased. this would be the correct answer </span>
<h2>Answer:</h2>
Arrangement of inter molecular forces from strongest to weakest.
- Hydrogen bonding
- Dipole-dipole interactions
- London dispersion forces.
<h3>Explanation:</h3>
Intermolecular forces are defined as the attractive forces between two molecules due to some polar sides of molecules. They can be between nonpolar molecules.
Hydrogen bonding is a type of dipole dipole interaction between the positive charge hydrogen ion and the slightly negative pole of a molecule. For example H---O bonding between water molecules.
Dipole dipole interactions are also attractive interactions between the slightly positive head of one molecule and the negative pole of other molecules.
But they are weaker than hydrogen bonding.
London dispersion forces are temporary interactions caused due to electronic dispersion in atoms of two molecules placed together. They are usually in nonpolar molecules like F2, I2. they are weakest interactions.
Answer:
A.
Explanation:
The <u>tertiary structure </u>of proteins is related to the interactions between the amino acids of the <u>primary structure</u>. Thus, these interactions give it a specific three-dimensional configuration which is very sensitive to <u>functionality</u>.
For example, <u>allosteric inhibitions</u> are related to this concept. When the <u>inhibitor</u> changes the tertiary structure of the protein it loses all <u>activity</u> and for the catalysis of the reaction.
Thus, the primary structure (which is related to the specific <u>sequence of amino acids</u>) will determine the tertiary structure since the chain folds will be a consequence of<u> intra-amino acid interactions</u>.
