How About a Nobel Prize for the Intelligent Designer?
Evolution News & Views
There's a simple logic about the Nobel Prize for Chemistry awarded this week, noted already here by David Klinghoffer: human attempts at engineering molecules to perform work are feeble imitations of what living cells have done perfectly since life first appeared on earth.
The Royal Swedish Academy of Science awarded the Nobel Prize in Chemistry to Jean-Pierre Sauvage (University of Strasbourg, France), Sir J. Fraser Stoddart (Northwestern University, Illinois), and Bernard L. Feringa (University of Groningen, the Netherlands) for their work in creating artificial molecular machines. All the news media have been talking about it, congratulating them on their well-deserved recognition. But think about how simple their designs are to date:
Sauvage in 1983 linked two molecular rings together.
Stoddart in 1991 "threaded a molecular ring onto a thin molecular axle and demonstrated that the ring was able to move along the axle."
Feringa in 1999 "got a molecular rotor blade to spin continually in the same direction."
The work, of course, didn't stop there. Stoddart used his little wheel and axle to design a tiny lift, an "artificial muscle" and a molecule-based computer chip. Feringa built a "nanocar" of sorts. It's pretty remarkable to be able to construct and direct a device that's 1,000 times smaller than the diameter of a human hair. Even though nobody has come up with the "killer app" yet, the Nobel Committee sees a lot of potential in these initial steps:
2016's Nobel Laureates in Chemistry have taken molecular systems out of equilibrium's stalemate and into energy-filled states in which their movements can be controlled. In terms of development, the molecular motor is at the same stage as the electric motor was in the 1830s, when scientists displayed various spinning cranks and wheels, unaware that they would lead to electric trains, washing machines, fans and food processors. Molecular machines will most likely be used in the development of things such as new materials, sensors and energy storage systems. [Emphasis added.]
Designers of these devices will undoubtedly use intelligence to get them to work properly. So then how did life's molecular machines originate? Nothing created by the winners even approaches the complexity and efficiency of life's molecular machines, which continue to challenge and fascinate the best minds in science.
The Nobel Prize Committee asked Bernard Feringa what inspired him to work on molecular machines. In the transcript from the phone call, interviewer Adam Smith asked him:
AS: So you describe your work as being inspired by nature?
BF: Ja, of course. If you look at the cells in our body or the functioning of the organism, it is flabbergasting. It is fantastic to see how this intricate machinery works. And when I'm taking about motors, as we focus on motors, if you look at the essential functions in the cell, like cell division, like transport, like making your muscles move, bacteria that go to food or [unclear ...] it's all controlled by molecular motors, and so the biological motors, and the biological machinery, is so crucial to all these functions. And of course we get great inspiration from that, while we as chemists are extremely good in building all kinds of materials, and that is what intrigued me.
The comparison is clear: three human designers of artificial machines were inspired by the "fantastic" and "flabbergasting" and "intricate" machinery going on inside the cells of their own bodies. They get to split a million dollars for their simple Lego-like constructions. What does the designer of the cell get?
In a word, insults. How would you like it if your best work was called a product of blind chance? That's essentially what two papers in the Proceedings of the National Academy of Science (PNAS) do when considering the origin of ATP synthase -- possibly the most efficient machine in the universe (see our animation).
In the first PNAS paper, "Biophysical comparison of ATP synthesis mechanisms shows a kinetic advantage for the rotary process," four researchers from the University of Pittsburgh basically say that ATP synthase evolved because rotation was more efficient.
The ATP synthase (F-ATPase) is a highly complex rotary machine that synthesizes ATP, powered by a proton electrochemical gradient. Why did evolution select such an elaborate mechanism over arguably simpler alternating-access processes that can be reversed to perform ATP synthesis? We studied a systematic enumeration of alternative mechanisms, using numerical and theoretical means. When the alternative models are optimized subject to fundamental thermodynamic constraints, they fail to match the kinetic ability of the rotary mechanism over a wide range of conditions, particularly under low-energy conditions. We used a physically interpretable, closed-form solution for the steady-state rate for an arbitrary chemical cycle, which clarifies kinetic effects of complex free-energy landscapes. Our analysis also yields insights into the debated "kinetic equivalence" of ATP synthesis driven by transmembrane pH and potential difference. Overall, our study suggests that the complexity of the F-ATPase may have resulted from positive selection for its kinetic advantage.
This is like saying that cars evolved wheels, tires, and shock absorbers because it makes them run better. Their "systematic enumeration of alternative mechanisms" sure didn't include intelligent causes.
The second paper, "Rotation of artificial rotor axles in rotary molecular motors," is even more flagrant in its design denial. Nine authors from universities in Tokyo think it was easy for a simple rotary engine to become an efficient rotary engine by chance.
F1/V1-ATPases are sophisticated molecular machines that convert the motion of a stator cylinder driven by sequential ATP hydrolysis to rotation of a central rotor protein. Here, we reveal the rotation of artificial rotor proteins composed of exogenous rod proteins that show no apparent sequence similarity with the native axles. The estimated torque by the artificial rotor in the stator ring of V1 was almost identical to that by the native axle protein. These results demonstrate that the principle of rotational motion by these molecular motors relies solely upon the coarse-grained interaction between the rotor and stator. These findings imply that the ancient F1 or V1 motor domain has evolved from a poorly designed motor protein more readily than initially assumed.
It implies no such thing. All their lab work was intelligently designed; on what basis can they conclude that some "ancient... poorly designed" motor got better by chance? They provide no mechanism by which that could happen, not even natural selection. Instead, they say, "the current consensus view of the field is that the interfaces of molecular motor systems have sophisticated designs at an atomic level through molecular evolution."
Yet the design principles are the same. Notice what Nature's congratulatory article says:
The Nobel winners' work -- and other chemists' nanomachines -- have also had an impact on researchers' understanding of nature, Astumian says. In particular, the artificial systems have helped to demonstrate that all chemically-powered molecular machines, whether synthetic or biological, work according to the same principles: by selectively harvesting the random jiggles of Brownian motion, rather than pushing against them.
Intelligent design theory, we repeat, cannot speak to the identity or nature of the designer. Our purpose here is to unmask the inconsistency in thinking by materialists. They will congratulate human designers of simple machines and give them millions of dollars for their highly gifted and intelligent work. But when it comes to awarding credit for molecular machines of far greater sophistication, they give the prize to "molecular evolution."
Evolution News & Views
There's a simple logic about the Nobel Prize for Chemistry awarded this week, noted already here by David Klinghoffer: human attempts at engineering molecules to perform work are feeble imitations of what living cells have done perfectly since life first appeared on earth.
The Royal Swedish Academy of Science awarded the Nobel Prize in Chemistry to Jean-Pierre Sauvage (University of Strasbourg, France), Sir J. Fraser Stoddart (Northwestern University, Illinois), and Bernard L. Feringa (University of Groningen, the Netherlands) for their work in creating artificial molecular machines. All the news media have been talking about it, congratulating them on their well-deserved recognition. But think about how simple their designs are to date:
Sauvage in 1983 linked two molecular rings together.
Stoddart in 1991 "threaded a molecular ring onto a thin molecular axle and demonstrated that the ring was able to move along the axle."
Feringa in 1999 "got a molecular rotor blade to spin continually in the same direction."
The work, of course, didn't stop there. Stoddart used his little wheel and axle to design a tiny lift, an "artificial muscle" and a molecule-based computer chip. Feringa built a "nanocar" of sorts. It's pretty remarkable to be able to construct and direct a device that's 1,000 times smaller than the diameter of a human hair. Even though nobody has come up with the "killer app" yet, the Nobel Committee sees a lot of potential in these initial steps:
2016's Nobel Laureates in Chemistry have taken molecular systems out of equilibrium's stalemate and into energy-filled states in which their movements can be controlled. In terms of development, the molecular motor is at the same stage as the electric motor was in the 1830s, when scientists displayed various spinning cranks and wheels, unaware that they would lead to electric trains, washing machines, fans and food processors. Molecular machines will most likely be used in the development of things such as new materials, sensors and energy storage systems. [Emphasis added.]
Designers of these devices will undoubtedly use intelligence to get them to work properly. So then how did life's molecular machines originate? Nothing created by the winners even approaches the complexity and efficiency of life's molecular machines, which continue to challenge and fascinate the best minds in science.
The Nobel Prize Committee asked Bernard Feringa what inspired him to work on molecular machines. In the transcript from the phone call, interviewer Adam Smith asked him:
AS: So you describe your work as being inspired by nature?
BF: Ja, of course. If you look at the cells in our body or the functioning of the organism, it is flabbergasting. It is fantastic to see how this intricate machinery works. And when I'm taking about motors, as we focus on motors, if you look at the essential functions in the cell, like cell division, like transport, like making your muscles move, bacteria that go to food or [unclear ...] it's all controlled by molecular motors, and so the biological motors, and the biological machinery, is so crucial to all these functions. And of course we get great inspiration from that, while we as chemists are extremely good in building all kinds of materials, and that is what intrigued me.
The comparison is clear: three human designers of artificial machines were inspired by the "fantastic" and "flabbergasting" and "intricate" machinery going on inside the cells of their own bodies. They get to split a million dollars for their simple Lego-like constructions. What does the designer of the cell get?
In a word, insults. How would you like it if your best work was called a product of blind chance? That's essentially what two papers in the Proceedings of the National Academy of Science (PNAS) do when considering the origin of ATP synthase -- possibly the most efficient machine in the universe (see our animation).
In the first PNAS paper, "Biophysical comparison of ATP synthesis mechanisms shows a kinetic advantage for the rotary process," four researchers from the University of Pittsburgh basically say that ATP synthase evolved because rotation was more efficient.
The ATP synthase (F-ATPase) is a highly complex rotary machine that synthesizes ATP, powered by a proton electrochemical gradient. Why did evolution select such an elaborate mechanism over arguably simpler alternating-access processes that can be reversed to perform ATP synthesis? We studied a systematic enumeration of alternative mechanisms, using numerical and theoretical means. When the alternative models are optimized subject to fundamental thermodynamic constraints, they fail to match the kinetic ability of the rotary mechanism over a wide range of conditions, particularly under low-energy conditions. We used a physically interpretable, closed-form solution for the steady-state rate for an arbitrary chemical cycle, which clarifies kinetic effects of complex free-energy landscapes. Our analysis also yields insights into the debated "kinetic equivalence" of ATP synthesis driven by transmembrane pH and potential difference. Overall, our study suggests that the complexity of the F-ATPase may have resulted from positive selection for its kinetic advantage.
This is like saying that cars evolved wheels, tires, and shock absorbers because it makes them run better. Their "systematic enumeration of alternative mechanisms" sure didn't include intelligent causes.
The second paper, "Rotation of artificial rotor axles in rotary molecular motors," is even more flagrant in its design denial. Nine authors from universities in Tokyo think it was easy for a simple rotary engine to become an efficient rotary engine by chance.
F1/V1-ATPases are sophisticated molecular machines that convert the motion of a stator cylinder driven by sequential ATP hydrolysis to rotation of a central rotor protein. Here, we reveal the rotation of artificial rotor proteins composed of exogenous rod proteins that show no apparent sequence similarity with the native axles. The estimated torque by the artificial rotor in the stator ring of V1 was almost identical to that by the native axle protein. These results demonstrate that the principle of rotational motion by these molecular motors relies solely upon the coarse-grained interaction between the rotor and stator. These findings imply that the ancient F1 or V1 motor domain has evolved from a poorly designed motor protein more readily than initially assumed.
It implies no such thing. All their lab work was intelligently designed; on what basis can they conclude that some "ancient... poorly designed" motor got better by chance? They provide no mechanism by which that could happen, not even natural selection. Instead, they say, "the current consensus view of the field is that the interfaces of molecular motor systems have sophisticated designs at an atomic level through molecular evolution."
Yet the design principles are the same. Notice what Nature's congratulatory article says:
The Nobel winners' work -- and other chemists' nanomachines -- have also had an impact on researchers' understanding of nature, Astumian says. In particular, the artificial systems have helped to demonstrate that all chemically-powered molecular machines, whether synthetic or biological, work according to the same principles: by selectively harvesting the random jiggles of Brownian motion, rather than pushing against them.
Intelligent design theory, we repeat, cannot speak to the identity or nature of the designer. Our purpose here is to unmask the inconsistency in thinking by materialists. They will congratulate human designers of simple machines and give them millions of dollars for their highly gifted and intelligent work. But when it comes to awarding credit for molecular machines of far greater sophistication, they give the prize to "molecular evolution."
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