Michael Cremo - Human Devolution - A Vedic Alternative To Darwin's Theory

1 in 1030 (10 followed by 30 zeroes). Also each amino acid molecule has a left handed L-form (from laevus, the Latin word for left) and a right handed D-form (from dexter, the Latin word for right). The two forms are mirror images of each other, like right and left shoes, or right and left gloves. In living things, all the proteins are composed of amino acid subunits of the L form. But L and D forms of amino acids occur equally in nature. To get a chain of 100 L-form amino acids, the odds again are 1 in

1030. This is equivalent to flipping a coin and getting heads one hundred times in a row. Therefore, the odds of getting a 100 amino acid chain with all peptide bonds and all L-form amino acids would be about 1 in 1060, which is practically zero odds in the available time limits.

Even if all the bonds are peptide bonds and all the amino acids are L forms, that is still not enough to give us a functional protein. It is not that any combination of amino acid subunits will give us a protein that will contribute to the function of a cell. The right amino acids must be arranged in quite specific orders (Meyer 1998, p. 126). The odds of the right 100 amino acids arranging themselves in the right order are in themselves quite high—about 1 in 1065 (the number of atoms in our galaxy is about 1065 ). Putting this more picturesquely, biochemist Michael Behe (1994, pp. 68–69) says that getting a sequence of 100 amino acids that functions as a protein is comparable to finding one marked grain of sand in the Sahara desert—three times in a row. If you put in the other factors (peptide binding, L-forms only) then the odds go up to 1 chance in 10125. So chance does not seem to work as an explanation for the chem……ical origin of life.

To avoid this conclusion, some scientists appeal to an infinite number of universes. But they have no proof that even one additional universe exists. Neither can they tell us if stable molecules form in any of these imaginary universes (stable molecules are necessary for the kind of life we observe in this universe). We shall consider this topic in greater detail in a later chapter.

Natural Selection

Some scientists, such as Oparin (1968, pp. 146–147), have proposed that natural selection could help select among amino acid chains to produce functional proteins, thus improving the odds that these proteins could form. In other words, protein formation does not rely on pure chance. But there are two problems with this. First, this prebiotic natural selection must operate on amino acid chains that were produced randomly, and we have already seen that the odds are very heavily against getting even a simple chain of amino acids with all peptide bonds and all L forms. So it would be hard to get even the basic raw materials (amino acid chains) upon which natural selection could operate. Second, natural selection involves some kind of molecular replication system. The odds that any such replication system could form by chance are even more remote than the odds against the chance formation of several kinds of amino acid chains upon which natural selection could act. The replication system itself must be made of combinations of highly specific complex protein molecules. Proposals such as Oparin’s therefore confront a major contradiction. Natural selection is supposed to produce the complex proteins, but natural selection requires a reliable molecular replication system, and all such systems known today are formed from complex and very specifically structured protein molecules. Oparin suggested that perhaps the earliest replication system did not have to be very reliable and that the system could make use of proteins that were not as specifically structured as proteins currently found in organisms. But Meyer (1998, p. 127) points out that “lack of . . . specificity produces ‘error catastrophes’ that efface the accuracy of self-replication and eventually render natural selection impossible.”

Despite these difficulties, Richard Dawkins (1986, pp. 47–49), in his book the Blind Watchmaker, still proposes that chance and natural selection (represented by a simple computer algorithm) can yield biological complexity. To demonstrate that the process is workable, he programmed a computer to generate random combinations of letters and compare them to a target sequence that forms an intelligible grammatically correct sentence. Those combinations of letters that come closest to the meaningful target sequence are preserved, whereas those that depart from the target sequence are rejected. After a certain number of runs, the computer produces the target sequence. Dawkins takes this as proof that random combinations of chemicals could by natural selection gradually produce biologically functional proteins. The reasoning is, however, faulty. First, Dawkins assumes the existence of a complex computer, which we do not find in nature. Second, he assumes the presence of a target sequence. In nature there is no target sequence of amino acids that is specified in advance, and to which random sequences of amino acids can be compared. Third, the trial sequences of letters that are selected by the computer do not themselves have any linguistically functional advantage over other sequences, other than that they are one letter closer to the target sequence. For the analogy between the computer algorithm and real life to hold, each sequence of letters chosen by the computer should itself have some meaning. In real life, an amino acid sequence leading up to a complex protein with a specific function should itself have some function. If it has no function, which can be tested for fitness by natural selection, there is nothing on which natural selection can operate. Meyer (1998, p. 128) says, “In Dawkins’s simulation, not a single functional English word appears until after the tenth iteration. . . . Yet to make distinctions on the basis of function among sequences that have no function whatsoever would seem quite impossible. Such determinations can only be made if considerations of proximity to possible future functions are allowed, but this requires foresight that molecules do not have.” In other words, Dawkins’s result can only be obtained because of the element of intelligent design embedded in the whole experiment.

Self-organization

Some scientists have suggested that something more than chance and natural selection is involved in the linking of amino acids to form proteins. They propose that certain chemical systems have self-organizing properties or tendencies. Steinman and Cole (1967) suggested that one amino acid may be attracted to another amino acid more than it is attracted to others. There is experimental evidence that this is true. There is some differential attraction among amino acids. Steinman and Cole claimed that the ordering of amino acids they observed in their experiments matched the ordering of amino acids in ten actual proteins. But when Bradley and his coworkers (Kok et al. 1988) compared the sequences reported by Steinman and Cole to a larger sample of sequences from 250 actual proteins, they found these 250 sequences “correlate much better with random statistical probabilities than with the experimentally measured dipeptide bond frequencies of Steinman and Cole” (Bradley 1998, p. 43). Also, if the properties of the twenty biological amino acids strongly determined the bonding of protein sequences we would expect only a few kinds of proteins to form, whereas we observe that thousands form (Bradley 1998, p. 43).

Another kind of self-organization happens when disordered molecules of a substance form crystals. This is technically called “spontaneous ordering near equilibrium phase changes.” The formation of crystals is fairly easy to explain. For example, when the temperature of water is lowered below the melting point, the tendency of water molecules to interact in a disordered way is overcome, and they link together in an ordered fashion. In this phase transition, the water molecules tend toward a state of equilibrium, moving to the lowest potential energy, giving up energy in the process. Imagine that there is a large depression in the middle of a billiards table. If you tilt the table here and there, the wandering balls will naturally wind up in the depression, touching each other and motionless. In the process energy is lost i.e. the process is exothermic. But the formation of complex biological molecules (biopolymers) is different. It is an endothermic process, meaning heat is added, and it takes place far from thermal equilibrium. The polymers are at a higher energy potential than their individual components. It is as if the pool table has a hump in the middle, rather than a depression. It is a lot more difficult to imagine all the balls winding up together on top of the hump simply as a result of random movement, than it is to imagine them winding up in the depression in a state of thermal equilibrium. It would take some energy to get the balls up on to the hump and keep them there. Bradley (1998, p. 42) says, “All living systems live energetically well above equilibrium and require a continuous flow of energy to stay there . . . Equilibrium is associated with death in the biosphere, making any explanationof the origin of life that is based on equilibrium thermodynamics clearly incorrect. . . . phase changes such as water freezing into ice cubes or snowflakes is irrelevant to the processes necessary to generate biological information.”