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An example of the protein-protein interactions is the antigen-antibody interactions. Because of the complexity of the protein molecules, the hydrophobic interactions are more dominant.

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Q: Why small molecule - protein interactions are generally domninated by hydrophobic interactions?
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What is hydrophobic and how do you determine if a molecule is hydrophobic?

Hydrophobic means that the molecule is repelled by water. You can tell if a molecule is hydrophobic by the way the atoms are arranged.


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Lipids are one of the four major macromolecules but they are NOT true polymers because their individual lipid molecules are NOT connected by covalent bonds. Instead one lipid molecule is connected to another lipid molecule by hydrophobic interactions.


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It breaks the hydrogen bonds and hydrophobic interactions between different parts of the protein molecule. Proteins are composed of amino acid subunits linked together by peptide bonds—this is called a polypeptide and is also known as the primary structure of a protein. The primary structure interacts with itself (also known as folding) forming hydrogen bonds and hydrophobic interactions with different parts of the same molecule. Heat disrupts the hydrogen bonds and hydrophobic interactions leaving the protein to unfold when it is heated. Since heat is not strong enough to break the peptide bonds between the amino acid subunits, the primary structure remains intact. Once the protein is cooled again, the hydrogen bonds and hydrophobic interactions can reform since they are based on the makeup of the primary structure and it hasn't changed. :) Hope this helps.


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