New Way to Measure Dark Energy

Researchers have discovered a method to potentially detect and measure dark energy by examining the motion between the Milky Way and Andromeda galaxies. This technique, still in its early stages, can estimate the upper value of the cosmological constant, a simple model of dark energy, which is five times higher than values determined from the early universe.




Researchers from the University of Cambridge have discovered a new way to measure dark energy – the mysterious force that makes up more than two-thirds of the universe and is responsible for its accelerating expansion – in our own cosmic backyard.

The researchers found that it may be possible to detect and measure dark energy by studying Andromeda, our galactic next-door neighbor that is on a slow-motion collision course with the Milky Way.


Since it was first identified in the late 1990s, scientists have used very distant galaxies to study dark energy but have yet to directly detect it. 

However, the Cambridge researchers found that by studying how Andromeda and the Milky Way are moving toward each other given their collective mass, they could place an upper limit on the value of the cosmological constant, which is the simplest model of dark energy. 

The upper limit they found is five times higher than the value of the cosmological constant that can be detected from the early universe.

Although the technique is still early in its development, the researchers say that it could be possible to detect dark energy by studying our own cosmic neighborhood. The results are reported in The Astrophysical Journal Letters.

Everything we can see in our world and in the skies – from tiny insects to massive galaxies – makes up just five percent of the observable universe. 

The rest is dark: scientists believe that about 27% of the universe is made of dark matter, which holds objects together, while 68% is dark energy, which pushes objects apart.  READ MORE...

Monks Riddled with Worms

A STUDY BY THE UNIVERSITY OF CAMBRIDGE HAS FOUND THAT MONKS WITHIN THE CAMBRIDGE AREA WERE ‘RIDDLED WITH WORMS’ DURING THE MEDIEVAL PERIOD.

The population of medieval Cambridge consisted of residents of monasteries, friaries and nunneries of various major Christian orders, along with merchants, traders, craftsmen, labourers, farmers, and staff and students at the early university.

The study published in the International Journal of Paleopathology revealed that the monks were twice as likely as ordinary townspeople to have high levels of intestinal worms. This is despite most Augustinian monasteries having far better sanitary conditions, latrine blocks and handwashing facilities, compared to the dwellings or ordinary working people.

A possible explanation for the parasitic infection may be down to monks using their own faeces, fertilisers containing human fertiliser, or pig excrement for manuring their crops in the friary gardens.

Cambridge archaeologists investigated samples of soil taken from around the pelvises of adult remains from the former cemetery of All Saints by the Castle parish church, as well as from the grounds where the city’s Augustinian Friary once stood.

Most of the parish church burials date from the 12-14th century, and those interred within were primarily of a lower socio-economic status, mainly agricultural workers.

The Augustinian friary in Cambridge was an international study house, known as a studium generale, where clergy from across Britain and Europe would come to read manuscripts. It was founded in the 1280s and lasted until 1538 before suffering the fate of most English monasteries: closed or destroyed as part of Henry VIII’s break with the Roman Church.  READ MORE...

Blue-Green Algae Powers Computer

Researchers from the University of Cambridge have managed to run a computer for six months, using blue-green algae as a power source.  A type of cyanobacteria called Synechocystis sp. PCC 6803 – commonly known as “blue-green algae,” which produces oxygen through photosynthesis when exposed to sunlight, was sealed in a small container, about the size of an AA battery, made of aluminum and clear plastic.

The research was published in the journal Energy & Environmental Science.  Christopher Howe from the University of Cambridge and colleagues claim that similar photosynthetic power generators could be the source of power for a range of small devices in the future, without the need for the rare and unsustainable materials used in batteries.

The computer was placed on a windowsill at one of the researchers' houses during the lockdown period due to COVID-19 in 2021, and stayed there for six months, from February to August.  The battery made of blue-green algae has provided a continuous current across its anode and cathode that ran a microprocessor.

The computer ran in cycles of 45 minutes. It was used to calculate sums of consecutive integers to simulate a computational workload, which required 0.3 microwatts of power, and 15 minutes of standby, which required 0.24 microwatts.  The microcontroller measured the device's current output and stored this data in the cloud for researchers to analyze.

Howe suggests that there are two potential theories for the power source. Either the bacteria itself produces electrons, which creates a current, or it creates conditions in which an aluminum anode in the container is corroded in a chemical reaction that produces electrons.  The experiment ran without any significant degrading of the anode and because of that, the researchers believe that the bacteria is producing the bulk of the current.

Further research is needed
Howe says that the approach could be scaled up, but further research is needed to figure out how far. He explains that putting one on your roof will not provide sufficient power for your house. But in rural areas of low and middle-income countries, in applications where a small amount of energy might be beneficial, such as environmental sensors or charging a mobile phone.  READ MORE...

Cause of Alzheimers

For the first time, researchers have used human data to quantify the speed
of different processes that lead to Alzheimer’s disease and found that it develops
in a very different way than previously thought. Their results could have
 important implications for the development of potential treatments.

The international team, led by the University of Cambridge, found that instead of starting from a single point in the brain and initiating a chain reaction that leads to the death of brain cells, Alzheimer’s disease reaches different regions of the brain early. How quickly the disease kills cells in these regions, through the production of toxic protein clusters, limits how quickly the disease progresses overall.

The researchers used post-mortem brain samples from Alzheimer’s patients, as well as PET scans from living patients, who ranged from those with mild cognitive impairment to those with late-stage Alzheimer’s disease, to track the aggregation of tau, one of two key proteins implicated in the condition.

In Alzheimer’s disease, tau and another protein called amyloid-beta build up into tangles and plaques – known collectively as aggregates – causing brain cells to die and the brain to shrink. This results in memory loss, personality changes, and difficulty carrying out daily functions.

By combining five different datasets and applying them to the same mathematical model, the researchers observed that the mechanism controlling the rate of progression in Alzheimer’s disease is the replication of aggregates in individual regions of the brain, and not the spread of aggregates from one region to another.

The results, reported in the journal Science Advances, open up new ways of understanding the progress of Alzheimer’s and other neurodegenerative diseases, and new ways that future treatments might be developed.

For many years, the processes within the brain which result in Alzheimer’s disease have been described using terms like ‘cascade’ and ‘chain reaction’. It is a difficult disease to study, since it develops over decades, and a definitive diagnosis can only be given after examining samples of brain tissue after death.

For years, researchers have relied largely on animal models to study the disease. Results from mice suggested that Alzheimer’s disease spreads quickly, as the toxic protein clusters colonize different parts of the brain.  READ MORE...

Tortoise Going in For The Kill

In what amounts to perhaps the most unhurried act of animal predation ever caught on camera, researchers have filmed for the first time a giant tortoise slowly – ever so slowly – closing in for the kill.

This drawn-out encounter – between a lumbering, almost leisurely giant tortoise (Aldabrachelys gigantea) and its grounded bird prey – is gruesome to watch. But it's also entirely transfixing.

After all, we've never seen a tortoise 'hunt' anything before. Who knew these dawdling giants had it in them?

"I couldn't believe what I was seeing," says biologist Justin Gerlach from the University of

Cambridge.  "It was horrifying and amazing at the same time."

  

The footage, captured on Frégate Island in the Seychelles archipelago, shows a female giant tortoise slowly pursuing a flightless lesser noddy tern (Anous tenuirostris) chick.

In a new study describing the encounter – said to be the "first documented observation of a tortoise deliberately attacking and consuming another animal" – the researchers indicate the hunt lasted seven minutes in total, including a passage where the tortoise pursued the chick along the top of a log.

The video – captured by Anna Zora, deputy conservation and sustainability manager with the Frégate Island Foundation – lasts for only a fraction of that, but it's enough to unequivocally show a deliberate, calculated attack on the part of the tortoise.  READ MORE

Using CRISPR

Can we reprogram existing life at will?

To synthetic biologists, the answer is yes. The central code for biology is simple. DNA letters, in groups of three, are translated into amino acids—Lego blocks that make proteins. Proteins build our bodies, regulate our metabolism, and allow us to function as living beings. Designing custom proteins often means you can redesign small aspects of life—for example, getting a bacteria to pump out life-saving drugs like insulin.

All life on Earth follows this rule: a combination of 64 DNA triplet codes, or “codons,” are translated into 20 amino acids.

But wait. The math doesn’t add up. Why wouldn’t 64 dedicated codons make 64 amino acids? The reason is redundancy. Life evolved so that multiple codons often make the same amino acid.

So what if we tap into those redundant “extra” codons of all living beings, and instead insert our own code?

A team at the University of Cambridge recently did just that. In a technological tour de force, they used CRISPR to replace over 18,000 codons with synthetic amino acids that don’t exist anywhere in the natural world. The result is a bacteria that’s virtually resistant to all viral infections—because it lacks the normal protein “door handles” that viruses need to infect the cell.

But that’s just the beginning of engineering life’s superpowers. Until now, scientists have only been able to slip one designer amino acid into a living organism. The new work opens the door to hacking multiple existing codons at once, copyediting at least three synthetic amino acids at the same time. And when it’s 3 out of 20, that’s enough to fundamentally rewrite life as it exists on Earth.

We’ve long thought that “liberating a subset of…codons for reassignment could improve the robustness and versatility of genetic-code expansion technology,” wrote Drs. Delilah Jewel and Abhishek Chatterjee at Boston College, who were not involved in the study. “This work elegantly transforms that dream into a reality.”  TO READ MORE, CLICK HERE...