2399 Thu 5 Oct 2017 INSIGHT-NET - FREE Online Tipiṭaka Research & Practice University and related NEWS through http://sarvajan.ambedkar.org in 105 languages http://sarvajan.ambedkar.org Google’s free service instantly translates words, phrases, and web pages between English and over 100 other languages. and render correct translation in your mother tongue for this google translation to attain Eternal Bliss as Final Goalhttps://www.google.co.in/amp/www.thehindu.com/sci-tech/science/molecules-shown-like-a-movie/article19797636.ece/amp/
Molecules shown like a movie
https://www-thehindu-com.cdn.ampproject.org/ii/w680/www.thehindu.com/sci-tech/science/article19797635.ece/alternates/FREE_435/TH05-UK-NOBEL2
Molecules shown like a movie
Nobel trio’s work helps in creating images of molecules
A trio of Swiss, American and British scientists won the 2017 Nobel chemistry prize on Wednesday for developing cryo-electron microscopy, allowing researchers to see biological molecules frozen in action.
The work by Jacques Dubochet, Joachim Frank and Richard Henderson makes it possible to image proteins and other molecules after freezing them rapidly to preserve their shape, providing a powerful new tool for medical research. “It’s like frames in a movie. Each of these pictures represents a frame and they can be put together into a movie and we can see what the molecules do,” said Peter Brzezinski, a member of the Nobel committee for chemistry.
The new approach fills a previously blank space by generating images of everything — from proteins that cause antibiotic resistance to the surface of the Zika virus. The Royal Swedish Academy of Sciences, which awarded the 9 million Swedish crown ($1.1 million) prize, said the technology had moved biochemistry into a new era.
By freezing biomolecules mid-movement, scientists can unravel previously unseen processes — a major advance both for basic understanding and the potential development of new drugs.
Scottish-born scientist Henderson used an electron microscope to generate a three-dimensional image of a protein at an atomic resolution, showing the potential of the technology.
His breakthrough was further developed by German-born scientist Frank, a U.S. citizen, while Dubochet of Switzerland used rapidly frozen water to preserve the natural shape of the biomolecules.
Mr. Frank said cryo-electron microscopy was a boon for medical research, which is increasingly focused on processes inside cells, but it would take time for this to play out — and he was taken aback by news of the award.
https://www.google.co.in/amp/indianexpress.com/article/explained/nobel-prize-in-chemistry-2017-jacques-dubochet-joachim-frank-richard-henderson-molecules-of-life-captured-in-3d-4874713/lite/
Nobel Prize in Chemistry, 2017: Molecules of life, captured in 3D
The use of cryo-electron microscopy, developed separately by the Laureates, allows biomolecules to be frozen mid-movement, and to be portrayed at atomic resolution. This technology, the Nobel Committee said, ‘has moved biochemistry into a new era’.
The 2017 Nobel Prize in Chemistry was on Wednesday awarded to Jacques Dubochet, Joachim
Frank and Richard Henderson “for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution”.
The electron microscope was designed in the early 1930s by the German physicist Ernst Ruska, for which he was awarded the 1986 Nobel Prize in Physics (along with Gerd Binnig and Heinrich Rohrer who shared the other half of the Prize). Four years earlier, the 1982 Chemistry Nobel had gone to Aaron Klug “for his development of crystallographic electron microscopy and his structural elucidation of biologically important nucleic acid-protein complexes”.
Through much of the first half of the 20th century, the determination of the structure of biomolecules — proteins, DNA and RNA — had appeared as a significant challenge in the field of biochemistry. Scientists’ knowledge evolved steadily over the last six decades — beginning with the pioneering crystallographic studies of the structures of globular proteins that fetched Max F Perutz and John C Kendrew the Chemistry Nobel in 1962, to mastering cryo-electron microscopy (cryo-EM) for which the 2017 Prize has been awarded.
In the 50s, X-ray crystallography (exposing protein crystals to X-rays) was used to develop models of biomolecules for research and development; in the 80s, nuclear magnetic resonance (NMR) spectroscopy was also employed to this end. The use of both techniques was, however, subject to limitations imposed by the nature of biomolecules. X-ray crystallography required well-organised crystals — biomolecules are usually never organised as crystals. And NMR worked for only a relatively small set of proteins.
The winners of the 2017 Prize employed three different approaches that together overcame these challenges, taking, as the Nobel Committee said, “biochemistry into a new era, making it easier than ever before to capture images of biomolecules”.