Final answer:
Enantiomers like L-DOPA and D-DOPA have the same chemical structure and properties; however, they differ in optical activity and biological function. The distinction is crucial in biochemical processes, as only specific enantiomers, such as L-amino acids, are used in protein synthesis. D-DOPA, being the enantiomer of L-DOPA, similarly shares many properties but will have different optical rotation and possibly different biological activities.
Step-by-step explanation:
When analyzing the properties of L-DOPA's enantiomer, D-DOPA, we must consider the principles of chirality and enantiomerism. Enantiomers, such as L-DOPA and D-DOPA, have nonsuperimposable mirror images due to their chiral centers. Despite sharing the same physical and chemical properties, they differ in their interaction with other chiral objects, such as biological receptors, and in their ability to rotate plane-polarized light.
The optical rotation is a critical distinguishing factor between enantiomers; L-DOPA will rotate plane-polarized light in one direction, whereas D-DOPA will rotate it to the same degree but in the opposite direction. Recall that physical properties like melting point, boiling point, and solubility are the same for enantiomers, but the direction of optical rotation differs, with the dextro or levo designation indicating the direction. It's also important to note that in biological systems, only certain enantiomers, like L-amino acids (which are actually dextro in optical activity), are utilized for protein synthesis.
One must remember that although L-amino acids correlate to the dextrorotary form in terms of optical activity, they do not always correspond to the upper case D-configuration descriptor, which is based on the configuration of atoms around the chiral carbon in the molecule. Thus, the enantiomer of L-DOPA, which is D-DOPA, will share many properties but differ in its biological activity and interaction with polarized light. Hence, while both L-DOPA and D-DOPA exist in nature, their interactions within biological systems and their effects on polarized light are distinct.