The Biology of Belief - Bruce H. Lipton [33]
Like other proteins, which we discussed earlier, receptors have an inactive and an active shape and shift back and forth between those conformations as their electrical charges are altered. When a receptor protein binds with an environmental signal, the resulting alteration in the protein’s electrical charges causes the backbone to change shape and the protein adopts an “active” conformation. Cells possess a uniquely “tuned” receptor protein for every environmental signal that needs to be read.
Some receptors respond to physical signals. One example is an estrogen receptor, which is specially designed to complement the shape and charge distribution of an estrogen molecule. When estrogen is in its receptor’s neighborhood, the estrogen receptor locks on to it, as surely as a magnet picks up paper clips. Once the estrogen receptor and the estrogen molecule bind in a perfect “lock and key” fit, the receptor’s electromagnetic charge changes and the protein shifts into its active conformation. Similarly, histamine receptors complement the shape of histamine molecules, and insulin receptors complement the shape of insulin molecules.
Receptor “antennas” can also read vibrational energy fields such as light, sound, and radio frequencies. The antennas on these “energy” receptors vibrate like tuning forks. If an energy vibration in the environment resonates with a receptor’s antenna, it will alter the protein’s charge, causing the receptor to change shape. (Tsong 1989) I’ll cover this more completely in the next chapter, but I’d like to point out now that because receptors can read energy fields, the notion that only physical molecules can impact cell physiology is outmoded. Biological behavior can be controlled by invisible forces, including thought, as well as it can be controlled by physical molecules like penicillin, a fact that provides the scientific underpinning for pharmaceutical-free energy medicine.
Receptor proteins are remarkable, but on their own they do not impact the behavior of the cell. While the receptor provides an awareness of environmental signals, the cell still has to engage in an appropriate, life-sustaining response, that is the venue of the effector proteins. Taken together, the receptor-effector proteins are a stimulus-response mechanism comparable to the reflex action that doctors typically test during physical examinations. When a doctor taps your knee with a mallet, a sensory nerve picks up the signal. That sensory nerve immediately passes on that information to a motor nerve that causes the leg to kick. The membrane’s receptors are the equivalent of sensory nerves, and the effector proteins are the equivalent of action-generating motor nerves. Together, the receptor-effector complex acts as a switch, translating environmental signals into cellular behavior.
It is only in recent years that scientists have realized the importance of the membrane’s IMPs. They are in fact so important that studying the way IMPs work has become a field of its own called “signal transduction.” Signal transduction scientists are busily classifying hundreds of complex information pathways that lie between the membrane’s reception of environmental signals and the activation of the cell’s behavior proteins. The study of signal transduction is catapulting the membrane to center stage, just as the field of epigenetics is highlighting the role of the chromosome’s proteins.
There are different kinds of behavior-controlling effector proteins because there are lots of jobs that need to be done for the smooth functioning of the cell. Transport proteins, for example, include an extensive family of channel proteins that shuttle molecules