Your Body's Molecular Machines

Joel Kontinen

This video is from 2017, but the science hasn’t changed that much.  It says that our body is wanderfully made, 

Molecular Machines Build Plant Cell Walls

Lignin makes trees grow upright.




Joel Kontinen

Plants are a lot more complicated than evolutionists are willing to admit. We can hardly chalk up their growth to Darwinian processes.

A paper published in Nature Plants discusses the molecular machinery that builds plant cell wall components.

Phys.org gives the gist of what goes on in plant cells:

“Two proteins embedded on membranes within plant cells serve as a scaffold to organize three key enzymes that specifically channel carbon into the synthesis of a cell-wall polymer called lignin.

Lignin is essential to plants' ability to grow upright and represents a substantial carbon-storage component of plants. But because it surrounds the other cell-wall components—cellulose and hemicellulose—lignin protects these carbon-rich substances from the biochemical processes commonly used to convert them to fuels or other bio-products.”

Building a plant gets quite complicated. While the three enzymes “are located near one another on a membrane known as the endoplasmic reticulum, they don't interact directly. Instead, two separate proteins interact with all three enzymes."

The endoplasmic reticulum is the “cell's interior ‘highway’ of membranes lined with the molecular machines that make proteins and transport those products within or out of cells.”

It should not be too difficult to see evidence of an intelligently designed system in all this. Molecular protein-making machines do not come about through trial and error. Designing them requires intelligence, as does the transportation business they’re involved in.

Human cells are even more amazing. They produce 100,000 nanomachines per hour and build miniature cities running at 100 percent efficiency.

Source:

Mcnulty Walsh, Karen. 2018. New details of molecular machinery that builds plant cell wall components. Phys.org (30 April).

Superfast Machine Production: 100,000 Nanomachines Per Hour in Our Cells

Image courtesy of LadyofHats, public domain.




Joel Kontinen

Recent research has likened our cells to “miniature cities running at 100 per cent efficiency.”

These cities and everything in them – including the tiny molecular motors dynein and kinesin – are assembled very fast.

A new study looks at ribosomes, which are amazing macromolecular machines. They, too, are built quickly from parts.

An article in Science Daily states:

“Consisting of RNA and proteins that twist, fold and turn [they] are responsible for making all of the protein within a cell and could hold the key to deciphering a range of diseases. Despite the intricacies of ribosomes, cells are able to churn out 100,000 of them every hour.”

Obviously, the parts are programmed to come together, otherwise the result would be a chaos.

Recently researchers at the Salk Institute for Biological Studies and The Scripps Research Institute used an imaging technique called single-particle cryo-electron microscopy (cryo-EM) to look into the secrets of how ribosomes are being built:

“In single-particle cryo-EM, proteins (the "particles") are flash-frozen and imaged using streams of electrons, meaning the molecules don't need to be crystallized and can retain much of their native structure.”

The research focused on the 50s subunit (a major component of ribosomes) and found that it was made up of “at least 15 types of complexes …13 of which are actively assembling 50s subunits.”

It took the scientists a year to figure this out.

No wonder integrated complex systems in cells are called supercomplexes.

They are the hallmark of exceptionally intelligent design.

Source:

Salk Institute.2016. Multi-institutional collaboration uncovers how molecular machines assemble. Science Daily (1 December).

Dynein: Tiny Tightrope Walking Machine in Our Cells

A dynein carrying cargo along a microtubule. Image courtesy of Wikipedia (Creative Commons Attribution 3.0 Unported license).




Joel Kontinen

Hardly a week goes by without a paper on molecular machines being published in a major science journal. Recently, PNAS published a study on the cytoplasmic dynein, which transports cargo by walking along a microtubule.

Fine-tuning is very much evident in its walk:

“Cytoplasmic dynein is the primary minus-end–directed microtubule (MT) motor. It is unclear how dynein coordinates ATP hydrolysis and MT attachment within and between its two motor domains, each containing four AAA+ ATPases (AAA: ATPase associated with various cellular activities), AAA1–4. We characterize how mechanical tension and nucleotide states of AAA1 and AAA3 regulate dynein–MT binding. Dynein binds MTs tighter when subjected to tension opposite its normal motility. ADP binding to AAA3 unexpectedly weakens MT-binding strength and reduces the bond strength anisotropy. Finally, AAA3 'gates' the activity of AAA1: ATP binding to AAA1 induces MT release only if AAA3 contains nucleotide. This work expands understanding of the role of force in dynein mechanochemistry and identifies regulatory functions of AAA3.”

A kinesin motor does practically the same thing, but in the opposite or plus-end direction. Both the dynein and kinesin suggest that our cells work in anything but a haphazard way.

In other words, fine-tuning and amazing design are evident from start to finish.

Source:

Nicholas, Matthew P. et al. 2015. Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosensing at multiple AAA domains. Proceedings of the National Academy of Sciences doi: 10.1073/pnas.1417422112