Today’s New Reason To Believe

Previously Posted on November 5th, 2007

Hugh Ross, Ph.D.

Sometimes the shortest path to learn about the scientific details of our planet Earth is to study similar details on other planets where the phenomena under investigation are simpler to investigate and understand. Mars is a good example of such a pathway. It also is a good example of how the study of other planets can expose hidden evidences for supernatural design in our own planet.

In a recent issue of Science a NASA astronomer, Norbert Schorghofer, develops a detailed model for the past forty ice ages on Mars.¹ Using measurements from satellites orbiting Mars, Schorghofer identified three different kinds of ice at the Martian poles: on top a dry layer, on the bottom a massive ice sheet, and in the middle a layer of pore ice. He also identified a large amount of subsurface ice at mid-latitudes.

Schorghofer demonstrated that the mid-latitude subsurface ice was well explained by large intermittent increases in the tilt of Mars’ rotation axis. His explanation implied that, unlike Earth, the main driving force behind Mars’ ice ages was changes in the tilt of its rotation axis. Schorghofer’s model showed that these changes were so dramatic and so rapid as to establish that over the past five million years Mars suffered forty ice age events, each event resulting in a wholesale climate change for the entire Martian surface.

If anything like the Martian experience occurred on Earth, all advanced and large-bodied life would be wiped out. Schorghofer’s study shows that dramatic and rapid climate changes by astronomical forcing (changes in the orbital and rotational characteristics) are the norm for planets. What makes Earth so extraordinary is that the variation in the tilt of its rotation axis is virtually nil and changes in the eccentricity and inclination of its orbit are very small compared to the other solar system planets. Evidently, Earth’s orbital and rotational features have been exquisitely fine-tuned to allow for the long-term survival of advanced life on its surface.

The degree of fine-tuning design in Earth’s orbital and rotational characteristics has become increasingly apparent and contributes to the conclusion that Earth and the solar system have been supernaturally and superintelligently manufactured to make human life and human civilization possible. Thanks to Schorghofer’s work, it should not be too long before scientists uncover even more evidence of God’s handiwork in the design of Earth and the solar system.

1. Norbert Schorghofer, “Dynamics of Ice Ages on Mars,” Nature 449 (September 13, 2007): 192-94.

Previously Posted on August 10th, 2007 by David H. Rogstad, Ph.D.

Continuing from last week, perusing 1 Corinthians 2:1-4 we notice that Paul chose not to come to them “with superiority of speech or of wisdom.”

¹And when I came to you, brethren, I did not come with superiority of speech or of wisdom, proclaiming to you the testimony of God. ²For I determined to know nothing among you except Jesus Christ, and Him crucified. ³I was with you in weakness and in fear and in much trembling, ⁴and my message and my preaching were not in persuasive words of wisdom, but in demonstration of the Spirit and of power (New American Standard Bible)

In the word “speech” he seems to refer to the method of his delivery, and in the word “wisdom” he refers to its content. As he explains later, by “wisdom” he means human wisdom—the wisdom of this age, not the wisdom of God. To appeal to the intellect of the Corinthians would be to appeal to their pride, for, as we have already mentioned, they were part of a culture that prided themselves in their oratory and philosophical pursuits. If Paul had used such an approach, they would be attracted to a false position in God’s kingdom. In order for them to genuinely come to Christ they would have to repent of their pride, not have it stirred up.

In order to receive God’s gift of life, they needed to repent. This repentance is not only from their moral failures. They must lose confidence in their independent, self-sufficient ways of thinking and come to a kind of “intellectual repentance.” We are told in many places in Scripture that human wisdom causes us to be puffed up with pride. For Paul to prepare an argument that appeals solely to the mind may, in fact, convince a mind, but he wants to do much more than simply convince them intellectually. He wants their hearts.

Now I am not suggesting that Paul never used well-prepared arguments to make his case for believing the gospel. He did it frequently in his discussions with Jews in the synagogues. Sound arguments supporting Christian truth-claims are necessary and can have a profound effect upon those who are prepared to hear and respond to them. As St. Augustine affirmed, reason itself doesn’t cause faith, but it everywhere supports faith. In this context, however, with a people who were so enamored with their own self-importance, Paul tells us in verse 2 that he “determined to know nothing among [them] except Jesus Christ, and Him crucified.”

What I think he is telling us here is that there are times when we must simply declare the truth of the gospel in its most fundamental terms, and leave the rest to God. To engage in debate on human wisdom can yield nothing but confusion and distraction from the real issues. Paul has already told us in chapter 1 that while the intellectual seeks for clever arguments and the religious seek for miraculous signs, God, in His wisdom, has chosen the method of preaching to save those who will believe (1:21-22). So this is the approach Paul takes with the Corinthians.

In verses 3 and 4, Paul repeats his description for emphasis in the form of two statements: instead of superiority of speech, he comes “in weakness and in fear and in much trembling”; and instead of persuasive words of wisdom, he comes “in demonstration of the Spirit and of power.” I see in Paul’s first statement a full recognition of his inability to convince the Corinthians through his own intellectual strengths. It is not so much that he feels unprepared but that he does not have the resources within himself to truly impress them—similar, perhaps, to his feelings in Athens. In his second statement, I see him wanting not just to convince their minds alone but to get into their very hearts and give them something that will convince them in their consciences.

We’ll see in next week’s post how Paul moves toward that goal.

Posted by Fazale ‘Fuz’ Rana, Ph.D.

Scientists Create Enzyme from Scratch

I have three teenage daughters who frustrate me to no end at times. I’m the type of person that likes to get where I’m going a few minutes early. And they never seem to be able to leave the house on time. Waiting for them to put on their make-up, fix their hair, choose the right outfit, etc. (who knows what else they do to get ready) seems to take an eternity. If only I could come up with a way to speed up the process. (I’ve discovered that standing at the bottom of the stairs yelling, “We are never going to get there if you don’t hurry up!” doesn’t work all that well.)

Not only am I an impatient parent, I’m also an impatient chemist. In fact, most chemists are in hurry. As part of their research efforts, these scientists often look for ways to speed up chemical reactions. Fortunately chemists have discovered a way to hustle things along. The rate of many chemical reactions can be accelerated by using compounds called catalysts.

The use of catalysts is not confined to the chemistry laboratory. They feature prominently in living systems as well. Most chemical reactions necessary for life are accelerated by special types of biological catalysts called enzymes. These biomolecules are proteins specifically structured to catalyze biochemical activities and operations. In some cases, enzymes can increase the rate of biochemical reactions by over a billion fold! If not for enzymes, life would be impossible because, without some assistance, most chemical transformations needed to sustain life proceed at too slow a pace under physiological conditions.

Whenever possible, chemists and chemical engineers take advantage of the special properties of enzymes for industrial, commercial, food, and agricultural applications. Scientists and technologists find enzymes useful because of their ability to accelerate chemical reactions with a high degree of chemical specificity. But there are also numerous problems with using enzymes for most large-scale applications. These biomolecules are not stable in organic solvents, or at high temperatures. Enzymes also have limited catalytic range, since not all types of chemical reactions are used by living systems.

In response to these deficiencies, biochemical engineers strive to redesign enzymes found in nature. They look to stabilize them under harsh conditions and extend their utility. (This endeavor is referred to as protein engineering.) Researchers also look to produce enzymes from scratch that will catalyze novel, nonbiological reactions.

Recently, a large team of collaborators published two papers in Science and Nature reporting on two enzymes, created from scratch and capable of catalyzing non-biological chemical transformations (the retro-aldol and the Kemp Elimination reaction, respectively).

Their work has several important implications. It paves the way for biochemists to develop a better understanding of the relationship between enzyme structure and function. It establishes an approach to generate novel enzymes with a wide array of practical applications. It also affects attempts by life scientists to create artificial life in the lab, and consequently, impacts the creation/intelligent design/evolution controversy. Before I discuss their work and its implications (next week), some background information will help.

Enzyme Structure

Enzymes are proteins. Proteins are chain-like molecules that fold into precise three-dimensional structures. The protein’s three-dimensional architecture determines its function.

Proteins form when the cellular machinery links together, in a head-to-tail fashion, smaller subunit molecules called amino acids. Cells employ twenty different amino acids to make proteins (to a first approximation). In principle, the twenty amino acids can link up in any possible amino acid combinations to form a protein chain.

The amino acids that make up the cell’s protein chains possess a variety of chemical and physical properties. Each amino acid sequence imparts the protein with a unique chemical and physical profile along its chain. This profile determines how the protein folds, and therefore, how it interacts with other protein chains to form a functional protein. The amino acid sequence of a protein ultimately determines its function, since the amino acid sequence determines the protein’s structure, and structure dictates function.

Enzyme Function

Even though enzymes are large molecules, only a small portion of their structure plays an immediate role in catalysis. The business portion of an enzyme is called the active site. Enzymes bind the chemical compounds destined to react with each other in the active site. Biochemists refer to these compounds as substrates. Once the chemical reaction is completed, the resulting products are released from the active site and more substrate molecules bind to the active site. This allows the enzyme to catalyze round after round of chemical reactions.

Enzyme active sites can only bind select molecules. In this way, enzymes have a high chemical specificity. This selectivity stems from the ability of the enzyme’s active site to precisely match the geometry of the substrate molecules and from the exacting molecular interactions that take place between the chemical groups found in the active site and the substrates.

The active site is typically a pocket or crevice located on the three-dimensional surface of the folded protein chain. The active site surface consists of a variety of chemical groups precisely positioned in space. These chemical groups come from amino acids that form the protein chain. Amino acids contributing to the active site may be located in completely different regions of the protein chain. They are brought into the appropriate juxtaposition when the protein chain folds into a three dimensional shape. (Go here for a close up of a typical enzyme active site.)

The spatial orientation of these chemical groups plays a critical role in the enzyme’s ability to speed up chemical reactions. These chemical groups stabilize the transition state of the enzyme substrates when they react and they shield the reactants from unwanted side reactions. Let me explain.

When molecules react, chemical bonds are broken and formed. Atoms within the molecule become redistributed. Chemical groups within and among the molecules temporarily associate and dissociate. These atomic-scale events proceed sequentially along what chemists call the reaction coordinate. At specific points along the reaction coordinate temporary molecular entities exist called transition states. Theses molecular configurations are unstable and are more energetic than either the original reactants or the final products. The less stable the transition state (or the higher the energy), the slower the reaction proceeds.

Chemical groups located within an enzyme’s active site are oriented in space in such a way that they interact with the reactants as they advance along the reaction coordinate. These interactions stabilize the transition states, lowering their energy. This allows the reactions to proceed at a more rapid rate.

Fine-Tuning of Enzyme Structure

Enzyme active sites are exquisitely fine-tuned molecular systems. Sometimes slight repositioning of active site chemical groups in space readily compromises the functional efficiency of enzyme-mediated catalysis.

As I point out in my new book The Cell’s Design over the last half-century, biochemists have discovered time and time again that molecular precision and fine-tuning define biochemical systems. Enzyme active sites are but one example. But the biochemical fine-tuning and exactness far exceed the best efforts of engineers.

Precision and fine-tuning are hallmark characteristics of intelligent design. These features dominate the best human designs and are often synonymous with exceptional quality. The fine-tuning and precision of enzyme active sites and other biochemical systems points to the work of a Divine Designer.

Next week I will describe what it takes to design an enzyme and its active site from scratch.