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Small-Scale Evidence of Grand-Scale Design

Dr. Hugh Ross, Ph.D.

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Hugh Ross launched his career at age seven when he went to the library to find out why stars are hot. Physics and astronomy captured his curiosity and never let go. At age seventeen he was the youngest person ever to serve as director of observations for Vancouver's Royal Astronomical Society. With the help of a provincial scholarship and a National Research Council (NRC) of Canada fellowship, he completed his undergraduate degree in physics (University of British Columbia) and graduate degrees in astronomy (University of Toronto). The NRC also sent him to the United States for postdoctoral studies. At Caltech he researched quasi-stellar objects, or "quasars," some of the most distant and ancient objects in the universe.

Not all of Hugh's discoveries had to do with astrophysics. He observed with amazement the impact of describing for people the process by which he came to personal faith in Jesus Christ. Some have expressed dismay but most have been overjoyed to meet someone who started at religious ground zero and through scientific and historical reality testing, became convinced that the Bible is truly the Word of God. He was stunned to discover how many individuals believed or disbelieved without checking evidence.

Hugh's unshakable confidence that God's revelation of Himself in Scripture and nature do not, will not, and cannot contradict became his unique message. Communicating that message as broadly and clearly as possible became his mission. He scouts the frontiers of origins research to share with scientists and nonscientists alike the thrilling news of what's being discovered and how it connects with biblical theology.

Between writing books and articles and recording the weekly television program Reasons to Believe, he travels around the world challenging high school and university audiences, churches and professional groups to consider the evidence for what they believe. He presents a persuasive case for Christianity without applying pressure. Because he treats people's questions and comments with respect, he is in great demand as a speaker and as a talk-radio and television guest.

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An array of new instruments is allowing researchers their closest-ever look at biomolecules’ inner workings.¹ This new view focuses all the way down to the atomic level. And the sights that meet biophysicists eyes are awe-inspiring, to say the least.

A group of Japanese scientists exploring the crystal structure of the F1-ATPase enzyme discovered nature’s own rotary engine —no bigger than ten billionths by ten billionths by eight billionths of a meter.² The tiny motor includes the equivalent of an engine block, a drive shaft, and three pistons. It runs at speeds between 0.5 and 4.0 revolutions per second. This motor not only ranks as the smallest ever seen, it also represents the smallest motor that the laws of physics and chemistry will allow.

In Germany, a research team used the new instruments to examine an enormous molecule, the yeast 26S proteasome.³ Though not the largest molecule in existence, the yeast 26S proteasome contains over two million protons and neutrons and is the largest non-symmetrical molecule mapped to date. This molecule can only be described as a "wonder." It serves as an intracellular waste-disposal and recycling system. Tiny molecules within the proteasome attach markers (called ubiquitin) to waste material (apparently the cell’s command center informs the marker molecules which proteins are ready for disposal). Since these ready-for-disposal proteins resemble tangled balls of yarn, the first job of the 26S proteasome, after identifying a tagged protein, is to unfold, untwist, and unravel it. This function is performed by an apparatus at each end of the proteasome.

Once the targeted protein is straightened out, the proteasome drags it into its core and cuts the protein into segments. These segments are precisely measured by a "ruler" inside the proteasome. The cut-up pieces are then ejected from the proteasome, and a "sanitation" fleet (other proteins) drives by to pick them up and sort them, separating the stuff that can be reused from the stuff that cannot.

The complexity of such systems—and these are just two of many—within both the tiny enzyme and the huge yeast reflect a mind-boggling quantity, not to mention quality, of information. Where did that information come from? Who structured these molecules and taught them to perform their functions? Did blind chance and random process? Are they simply self-programmed? Does anything in reality self-program without intelligent input?

I see these discoveries as a formidable challenge to the assumption that life arose on its own over a few million years.⁴ Perhaps at least some scientists will be prompted by the new data to reconsider their conclusion, to accept the possibility—more accurately, the probability—that living molecules and all living creatures evidence the matchless brilliance and power of a Supreme Creator.

References

1. Steven M. Block, "Real Engines of Creation," Nature , 386 (1997), pp. 217-219.
2. Hiroyuki Noji, Ryohei Yasuda, Masasuke Yoshida, and Kazuhiko Kinosita Jr., "Direct Observation of the Rotation of F1-ATPase," Nature, 386 (1997), pp. 299-302.
3. Michael Groll et al, "Structure of 20S Proteasome from Yeast at 2.4 A° Resolution," Nature, 386 (1997), pp. 463-471.
4. Hugh Ross, "New Evidence of Old Life," Facts & Faith, v. 11, n. 1 (1997),pp.3-4.

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Updated: 14 December 2002