Answer :
The argument that provides evidence that best explains the interaction between an enzymatic protein and its substrate as a chemical reaction takes place is - the enzyme has a specific structure so that only one substrate can bind to it. As the enzyme and substrate come together, the shape of each perfectly complements the other.
Hence, the correct option is A.
Proteins called enzymes are made up of amino acids connected by one or more polypeptide chains. The fundamental structure of a polypeptide chain refers to this arrangement of amino acids. This in turn dictates the geometry of the active site and the three-dimensional structure of the enzyme.
An enzyme-substrate complex is created when an enzyme binds to its substrate. This complex provides certain ions or chemical groups that really establish covalent bonds with molecules as a crucial stage of the reaction process, lowering the activation energy of the reaction and promoting its quick advancement.
The substrate is bound by the enzyme's active site. Because enzymes are proteins, this region has a special arrangement of amino acid residues (side chains or R groups). Every residue of an amino acid can be big, tiny, weakly basic or acidic, hydrophilic or hydrophobic, positively, negatively, or neutrally charged, or it can be neutral.
The complete question is:
Which argument provides evidence that best explains the interaction between an enzymatic protein and its substrate as a chemical reaction takes place?
A
The enzyme has a specific structure so that only one substrate can bind to it. As the enzyme and substrate come together, the shape of each perfectly complements the other
B
The enzyme has a specific chemical composition so that only one substrate can bind to it. The chemicals in the enzyme and substrate cause them to be attracted to each other
C
The enzyme has a specific chemical composition so that only one substrate can bind to it. The chemicals in the enzyme cause the components of the substrate to be repelled from each other
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