Bob Hosken, biochemistry
Dr. Hosken is senior lecturer in food technology at the University of Newcastle, Australia. He holds a B.S. in biochemistry from the University of Western Australia, an M.S. in biochemistry from Monash University, a Ph.D. in biochemistry from the University of Newcastle and an M.B.A. from the University of Newcastle. Dr. Hosken has published more than 50 research papers in the areas of protein structure and function, food technology, and food product development.
My first year at university was one of the most challenging and exciting times in my life. Suddenly I was no longer a child; I was independent, having to interpret the world for myself, planning my own future and determining my own life values. I was unsure of what I should study, and my high school peer group disintegrated as some friends chose to study arts, while others went into law, dentistry, or commerce. While I had many memorable lectures in the first year, some of which are best forgotten, it was the one lecture on glycolysis and the Krebs cycle which stood out, opening up to me a whole new world: the marvels of biochemistry and molecular biology. I found the metabolic steps involved in the synthesis and release of chemical energy through photosynthesis and oxidative phosphorylation—absolutely marvellous. I could not get enough of it, I had to become a biochemist.
In this subject we also had several lectures on evolutionary biology, and while the concepts were interesting, they did not excite me intellectually or emotionally. To me, unlocking the secrets of metabolism was like opening the book of life. There had to be a designer for this system to work, and to me this was not chance, but the hand of God.
After graduating in chemistry and biochemistry, I began my postgraduate career, focusing on the biosynthesis, structure, and function of proteins. I worked with a team to determine the amino acid sequences of myoglobin and hemoglobin from a range of Australian marsupials and monotremes, with the aim of determining the phylogenetic relationships of these unique animals. Marsupials are pouched animals and include the kangaroos, while the monotremes lay eggs and include the echidna and the platypus, and it is these features that make the latter so interesting to the taxonomist. Given that the platypus lays eggs, has a duck-like beak, webbed feet, and a furry tail, it is not surprising that some people have viewed it as a missing link in the evolution of animals.
It was found that the amino acid sequences for myoglobin and hemoglobin from various species of kangaroo, echidna, and platypus were different, and the sequence information could be used to evaluate the phylogenetic relationships of these animals. This could then be linked to the radiation of animals associated with continental drift and the evolutionary record.
While these findings were very interesting, the most exciting thing for me about this work was the opportunity it provided for relating the molecular architecture of each species of hemoglobin to the unique physiological requirements of the animal species studied.
In other words, in a study of the relation between the structure and function of hemoglobin in various marsupial and monotreme species, I found it more meaningful to interpret hemoglobin structure in relation to the unique physiological demands of each species. A marsupial mouse has a greater rate of metabolism than a large kangaroo, so small marsupials need a hemoglobin with a structure designed to deliver oxygen to the tissues more efficiently than that required in large animals, and I found this to be actually the case. I also investigated the relation of hemoglobin structure and oxygen transport in the echidna and platypus, and again found the oxygen delivery system of the platypus was well suited to diving, while in the echidna it was suited to burrowing. The bill of the platypus has been found to be equipped with incredibly sensitive electroreceptors, capable of sensing muscular contraction of tiny prey, including dragonfly or mayfly larvae. This enables the platypus to find food in the murky waters in which it lives. These kinds of findings indicate to me that each animal is in some way uniquely designed to suit its particular environment, and I cannot help but attribute the complexity of the design to a Creator, rather than to random evolutionary forces.
The argument of design in nature as an evidence for a Creator is not new. William Paley, in his Natural Theology in the 1860s, used this kind of general argument. He was, however, not able to draw on the insights provided by modern molecular biology. While these arguments are in part based on nonscientific paradigms, what’s new? Most people, in fact, make their most important decision in life on nonscientific paradigms. Today as we ponder the unique architecture of the molecular systems that make up life, I am sure that I will not be the last person to conclude that “there must be an architect.”
I have regarded my early research experience in the area of protein structure and function as a privilege, not only because it provided me with wonderful insights into molecular design and function, but also because it provided the insights to appreciate the subsequent advances that were to take place in biochemistry and molecular biology. I could now appreciate more than ever the complexity of the molecular control mechanism involved in metabolism and the immunological defense systems of the body. The one-hour lecture in first year university studies of glycolysis and the Krebs cycle, which had initiated my interest in biochemistry, could now be expanded to fill many books, and I cannot possibly conceive how such a system could ever evolve. There has to be an intelligent designer, and this is my personal God. http://www.answersingenesis.org/home/Area/isd/hosken.asp