Earth-like planets

If extraterrestrial life does exist in outer space, planet KOI-172.02 is a good candidate to host life similar to that on Earth. Using the Kepler space telescope to find planets, scientists at NASA have detected at least 17 billion Earth-like planets surrounding Sun-like stars in the Milky Way. Kepler detects potential alien worlds by watching for significant dips in starlight, created when planets pass in front of their parent stars. This January, a fresh analysis of data from NASA’s Kepler mission, launched in 2009, suggests that about 17 per cent of all the sun-like stars in the Milky Way host a rocky planet similar in composition to Earth.

The planet KO1-172.02 is a super Earth-size planet candidate, which means it is 1.25-2 times the size of the Earth. It has an orbit of 150 days or less, placing it in the habitable zone—the region around a star where liquid water might exist on the surface of a planet. When planets are found in these regions, the conditions are favourable for life.

According to the data collected, scientists have concluded that nearly all stars similar to our sun have planets—many of which resemble the Earth in terms of composition and orbit. Kepler mission project scientist Steve Howell told CBC, “It is no longer a question of if we will find a true Earth analogue, but a question of when.”

Volcano eruptions

When Mount Etna, the highest active volcano in Europe, erupts, the sky takes on an orange glow. It spews molten rock hundreds of metres into the air, creating a fiery display of lava cascading down the sides of the volcano.

Although scientists do not fully understand the mechanisms controlling the magnitude of the 50 to 60 volcanic eruptions that occur worldwide each year, McGill University’s department of Earth and planetary sciences Professor Don R. Baker recently discovered a small but important step in being able to predict the type of eruption that could occur.

Volcanic eruptions are driven by the rapid expansion of bubbles formed from water and other volatile substances trapped in the molten rock as it rises beneath the volcano. Working on an international research team, Baker and his colleagues discovered that the difference between a large or small eruption depends on the first 10 seconds of bubble growth in molten rocks.

To examine the growth of volcanic bubbles, Baker and his colleagues heated water-bearing molten rock with a recently developed laser heating system. By performing CAT scans on the samples during the first 18 seconds of bubble growth, they were able to characterize the bubbles by size distribution.

By studying the samples, Baker has found a possible link between the size distribution of the bubbles and the eruptive behaviour of the volcano. Depending on the type of bubbles that form, they trap gas inside of them, and are swiftly combined into a foam with eruptive behaviour.

These findings suggest the need to develop volcanic monitoring systems to measure rapid changes in gas flux and composition during critical points in time. With such a system, scientists may one day be able to predict the type of volcanic activity expected from the world’s volcanoes.

Immune system protein discovered

The immune system is composed of defender molecules, which act as foot soldiers to guard the body against infection. Researchers at McGill University and the Research Center for Molecular Medicine of the Austrian Academy of Sciences have recently discovered how one such protein, IFIT, functions. The findings could help advance the development of new drugs to combat immune system disorders. Further, this discorvery might provide insight into dampening the immune response when necessary, such as for inflammation or cancer therapy.

IFIT is a key protein in the human immune system that detects viruses and latches onto them in order to prevent infection. In order to recognize a virus from a normal host cell, IFIT depends on the RNA. When a virus enters the cell, it generates foreign RNA molecules that differ from the RNA found in a human. The researchers determined that IFIT proteins have evolved a specific binding pocket, that will only fit the foreign RNA of viruses. Through this pocket, the IFIT protein clamps down on the viral RNA. By binding to the RNA, IFIT prevents the virus from replicating, thereby arresting the infection.