In every remote corner of the world there are people like Carl Jones and Don Merton who have devoted their lives to saving threatened species. Very often, their determination is all that stands between an endangered species and extinction.But why do they bother? Does it really matter if the Yangtze river dolphin, or the kakapo, or the northern white rhino, or any other species live on only in scientists' notebooks?Well, yes, it does. Every animal and plant is an integral part of its environment: even Komodo dragons have a major role to play in maintaining the ecological stability of their delicate island homes. If they disappear, so could many other species. And conservation is very much in tune with our survival. Animals and plants provide us with life-saving drugs and food, they pollinate crops and provide important ingredients or many industrial processes. Ironically, it is often not the big and beautiful creatures, but the ugly and less dramatic ones, that we need most.Even so, the loss of a few species may seem irrelevant compared to major environmental problems such as global warming or the destruction of the ozone layer. But while nature has considerable resilience, there is a limit to how far that resilience can be stretched. No one knows how close to the limit we are getting. The darker it gets, the faster we're driving.There is one last reason for caring, and I believe that no other is necessary. It is certainly the reason why so many people have devoted their lives to protecting the likes of rhinos, parakeets, kakapos, and dolphins. And it is simply this: the world would be a poorer, darker, lonelier place without them.
To establish evolutionary interrelatedness invariably requires exhibiting similarities between organisms. Within Darwinism, there's only one way to connect such similarities, and that's through descent with modification driven by the Darwinian mechanism. But within a design-theoretic framework, this possibility, though not precluded, is also not the only game in town. It's possible for descent with modification instead to be driven by telic processes inherent in nature (and thus by a form of design). Alternatively, it's possible that the similarities are not due to descent at all but result from a similarity of conception, just as designed objects like your TV, radio, and computer share common components because designers frequently recycle ideas and parts. Teasing apart the effects of intelligent and natural causation is one of the key questions confronting a design-theoretic research program. Unlike Darwinism, therefore, intelligent design has no immediate and easy answer to the question of common descent.Darwinists necessarily see this as a bad thing and as a regression to ignorance. From the design theorists' perspective, however, frank admissions of ignorance are much to be preferred to overconfident claims to knowledge that in the end cannot be adequately justified. Despite advertisements to the contrary, science is not a juggernaut that relentlessly pushes back the frontiers of knowledge. Rather, science is an interconnected web of theoretical and factual claims about the world that are constantly being revised and for which changes in one portion of the web can induce radical changes in another. In particular, science regularly confronts the problem of having to retract claims that it once confidently asserted.
In describing a protein it is now common to distinguish the primary, secondary and tertiary structures. The primary structure is simply the order, or sequence, of the amino-acid residues along the polypeptide chains. This was first determined by [Frederick] Sanger using chemical techniques for the protein insulin, and has since been elucidated for a number of peptides and, in part, for one or two other small proteins. The secondary structure is the type of folding, coiling or puckering adopted by the polypeptide chain: the a-helix structure and the pleated sheet are examples. Secondary structure has been assigned in broad outline to a number of librous proteins such as silk, keratin and collagen; but we are ignorant of the nature of the secondary structure of any globular protein. True, there is suggestive evidence, though as yet no proof, that a-helices occur in globular proteins, to an extent which is difficult to gauge quantitatively in any particular case. The tertiary structure is the way in which the folded or coiled polypeptide chains are disposed to form the protein molecule as a three-dimensional object, in space. The chemical and physical properties of a protein cannot be fully interpreted until all three levels of structure are understood, for these properties depend on the spatial relationships between the amino-acids, and these in turn depend on the tertiary and secondary structures as much as on the primary. Only X-ray diffraction methods seem capable, even in principle, of unravelling the tertiary and secondary structures.[Co-author with G. Bodo, H. M. Dintzis, R. G. Parrish, H. Wyckoff, and D. C. Phillips]