The overall shape of an enzyme changes after the attachment with the substrate.
Enzymes are proteins composed of amino acids that linked together in one or more polypeptide chains. This sequence of amino acids in the form of polypeptide chain is known as the primary structure of an enzyme.
The tertiary structure is the enzyme's overall three dimensional structure, which occurs due to interactions between the R groups of the amino acids that make up the protein and the active sites of the substrate with which the enzyme can attach so we can conclude that the overall shape of an enzyme changes after the attachment with the substrate.
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The primary structure of enzymes determinies their functions and their secondary and tertiary structures. R groups remain in the center of the molecule and stabilize the structure.
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To answer this question, we need to remember that enzymes are proteins, and hence, they share many properties. From now on, we will refer to the enzyme as proteins or molecules.
Amino acids are organic molecules. They are composed of a central carbon, one hydrogen atom, one carboxyl group (COOH), one amine group (NH2), and one R group.
The composition of the R group is what makes them different from each other.
Proteins are amino acid polymers linearly arranged and connected by peptidic bonds. These molecules characterize by their different structures.
The peptidic bond is the union of two amino acids by their carboxyl and amine groups.
The R group of each amino acid is involved in stabilizing the molecule through their interactions.
The amount of amino acids that compose the polypeptide and their order in the chain determines the primary structure of the protein. The primary structure of the proteins determines the tertiary one.
Protein functions also depend on the aminoacids sequences. Proteins with different functions have different sequences. And among species, proteins with similar functions have similar structures.
The primary structure refers to the sequence in which the amino acids are arranged in the chain.
The secondary structure is the folding that the polypeptide chain adopts thanks to the formation of hydrogen bonds.
The three-dimensional structure makes them even more stable in the environment and capable of properly accomplishing their biological role.
When proteins are composed of more than one polypeptide subunit, they arrange in a fourth structure, named quaternary structure.
The hydrophilic R-groups remain in the center of the molecule, facing the protein interior, and avoiding interaction with water.
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