Receptors are molecular "antennas" that recognize environmental signals. Some receptor antennas extend inward from the membrane’s cytoplasmic face. These receptors "read" the internal milieu and provide awareness of cytoplasmic conditions. Other receptors extending from the cell’s outer surface provide awareness of external environmental signals.

Conventional biomedical sciences hold that environmental "information" can only be carried by the substance of molecules (Science 1999, 284:79-109). According to this notion, receptors only recognize "signals" that physically complement their surface features. This materialistic belief is maintained even though it has been amply demonstrated that protein receptors respond to vibrational frequencies. Through a process known as electroconformational coupling (Tsong, Trends in Biochem. Sci. 1989, 14:89-92), resonant vibrational energy fields can alter the balance of charges in a protein. In a harmonic energy field, receptors will change their conformation. Consequently, membrane receptors respond to both physical and energetic environmental information.

A receptor’s "activated" conformation informs the cell of a signal’s existence. Changes in receptor conformation provide for cellular "awareness." In its "activated" conformation, a signal-receiving receptor may bind to either a specific function-producing effector protein or to intermediary processor protein. Receptor proteins return to their original "inactive" conformation and detach from other proteins when the signal ceases.

The family of effector proteins represent "output" devices. There are three different types of effectors, transport proteins, enzymes and cytoskeletal proteins. Transporters, which include the extensive family of channels, serve to transport molecules and information from one side of the membrane barrier to the other. Enzymes are responsible for metabolic synthesis and degradation. Cytoskeletal proteins regulate the shape and motility of cells.

Effector proteins generally possess two conformations: an active configuration in which the protein expresses its function; and a "resting" conformation in which the protein is inactive. For example, a channel protein in its active conformation possesses an open pore through which specific ions or molecules traverse the membrane barrier. In returning to an inactive conformation, protein refolding constricts the conducting channel and the flow of ions or molecules ceases.