. Supposedly, the ancient original myoglobin molecules slowly evolved along two paths until the precisely designed a- and b- haemoglobin molecules resulted that function only when linked together in groups of four to work in the blood in a much different way under very different conditions from myoglobin in the muscle cells. What we have today in modern myoglobin and haemoglobin molecules are marvels of perfect designs for special, highly demanding tasks. Is there any evidence that intermediate, half-evolved molecules could have served useful functions during this imaginary evolutionary change process, or that any creature could survive with them in its blood? There is no such information. Modern vertebrates can tolerate very little variation in these molecules. Thus, the supposed evolutionary history of the allegedly homologous globin molecules is a fantasy, not science.1
As Dr. Kofahl makes clear, the NAS's claims regarding molecular homology are not science at all, but merely fantasy, like all its other claims.
Moreover, the evolutionists' accounts fail to explain the origin of the myoglobin protein. They say that hemoglobin evolved from myoglobin, but how myoglobin came into existence is still a mystery to them.
Molecular Comparisons Conflict with The So-Called Family Tree
It is suggested in Science and Creationism that an evolutionary family tree can be drawn up by comparing the proteins in living things, such as hemoglobin, myoglobin, or cytochrome c, and that this tree will agree with the paleontological and anatomical facts. This claim is set out in these terms:
The so-called family trees obtained from analyses of such molecules as hemoglobin, myoglobin, and cytochrome c conflict both with one another and with other data.
It is astonishing that the NAS should make such a claim, ignoring important research and findings in this area. In actuality, comparisons of the molecules cited by the NAS actually represent enormous difficulties for the theory of evolution and reveal its inconsistencies. Before examining the contradictions and errors of the NAS and the theory of evolution in this area, let us provide some information about molecular comparisons.
The protein molecules on which the structures and functions of living things depend consist of amino acids. There are 20 kinds of amino acids in proteins. One particular sequence of amino acids might give rise to a fat-digesting protein in the stomach, while another chain of amino acids might cause an oxygen-binding protein molecule to form. Generally speaking, the amino-acid sequence is the same for the same kind of protein in the same species. However, the amino-acid sequence can change between species. This is the case, for instance, with the hemoglobin molecule, which allows oxygen to be carried in the blood. The practice of comparing the differences in a particular protein molecule between species in order to draw conclusions about evolutionary relationships is known as "molecular homology." For instance, the amino-acid sequences of the hemoglobin molecules in human beings, mice, and horses can be identified and compared. According to evolutionists, the protein sequences of species assumed to have a closer evolutionary relationship should be closer to one another. For instance, the sequences in the hemoglobins of human beings and horses should be closer to each other than to those of rats. Yet, research in this field has revealed a conflict between comparisons at the molecular level and the claims of the theory of evolution. Following are some of the research conclusions that have revealed this contradiction:
• Comparisons carried out on the molecule cytochrome c, cited by the NAS as evidence for evolution, resulted in disappointment for evolutionists. These comparisons showed that the turtle was closer to birds than to the snake, another reptile. Evolutionists had claimed that the protein sequences of the turtle and snake, two reptiles, should be much closer to each another. 2
•The same research also revealed that chickens exhibit greater similarities to penguins 