What breakthrough technology might be awarded the 2017 Nobel Prize in Chemistry?

In summary: I will list CRISPR as the favorite for the award.Official prediction:Franz-Ulrich Hartl and Arthur Horwich for their discoveries of chaperone-assisted protein foldingIn summary, the 2017 Nobel Prize in Chemistry will be announced tomorrow and there is speculation that it may be awarded for works on nanotechnology. However, it is unlikely as last year's prize was awarded for work in the same field. The top predictions for the prize are for discoveries in epigenetics, specifically the chemical modification of histone proteins, and for the discovery of CRISPR-Cas9 and its application to genome editing. Other potential winners include Franz-U
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ISamson
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The 2017 Nobel Prize in Chemistry is being announced tomorrow!
I really can't wait to see what it will be awarded for, because it is always interesting and sometimes unexpected.
I think it might be awarded for works on nanotechnology, because it is currently a hot field.
It might be displayed live on youtube and the Nobel Prize website.
I am looking forward to it!

https://www.nobelprize.org/
 
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  • #2
Ivan Samsonov said:
The 2017 Nobel Prize in Chemistry is being announced tomorrow!
I really can't wait to see what it will be awarded for, because it is always interesting and sometimes unexpected.
I think it might be awarded for works on nanotechnology, because it is currently a hot field.

Given that last year's prize for work on molecular motors was for work in the field of nanotechnology, I doubt they would make another award in the field of nanotechnology this year. However, the next time they decide to award the prize for work in nanotechnology, what discoveries and what people do you think would be worthy or honoring.

Here's my predictions (all lean towards biology as that's what I'm most familiar with):
Personal prediction (who I would want to win):
Michael Grunstein, C. David Allis, and Stuart Schreiber for their discoveries concerning the chemical modification of histone proteins in gene regulation
Why they won't win: The general field of "epigenetics" has definitely had a huge impact on biomedical research, but it is one that suffers from the rule that at most three individuals can be honored. There are just too many people who have contributed to this field for the prize to be awarded without controversy.

Who most people are predicting:
Emmanuel Charpentier, Jennifer Doudna, and Feng Zhang for their discovery of CRISPR-Cas9 and its application to genome editing
Why they won't win: For this prize, it's not a matter of if they will win, but when they will win (though the prize may or may not include Zhang). Since Charpentier and Doudna's key publication in 2012, CRISPR has revolutionized biomedical science. Even if it has not yet made its way into any clinical applications, CRISPR has enabled a number of major discoveries in research and would deserve the prize just for its utility as a research tool. However, the Nobel Committee likes to wait before making its awards. The last slam-dunk prizes (discovery of RNA interference and induced pleuripotent stem cells), had to wait eight years and six years between discovery and awarding of the prize. Maybe in 2018 (six years after the key 2012 publication), I will list CRISPR as the favorite for the award.

Official prediction:
Franz-Ulrich Hartl and Arthur Horwich for their discoveries of chaperone-assisted protein folding
These two were recognized for their work in this field by a Lasker Award in 2011, which can often be a precursor to a Nobel Prize. Their major discoveries were done in the late 1980s and early 1990s and their work is a standard part of biology and biochemistry textbooks, yet it has not yet been recognized by the Nobel Committee. Unlike with epigenetics, there seems to be consensus that these two individuals deserve the credit for the key discoveries in this field. As protein misfolding plays a role in many diseases (such as Alzhemier's, Huntington's, and ALS), their work has been critical toward working to better understand and treat these conditions. The passing of Sue Lindquist, another giant in the field of protein folding, in late 2016 should hopefully serve as a reminder to the Committee to recognize this field.
 
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  • #3
Ygggdrasil said:
Given that last year's prize for work on molecular motors was for work in the field of nanotechnology, I doubt they would make another award in the field of nanotechnology this year. However, the next time they decide to award the prize for work in nanotechnology, what discoveries and what people do you think would be worthy or honoring.

Here's my predictions (all lean towards biology as that's what I'm most familiar with):
Personal prediction (who I would want to win):
Michael Grunstein, C. David Allis, and Stuart Schreiber for their discoveries concerning the chemical modification of histone proteins in gene regulation
Why they won't win: The general field of "epigenetics" has definitely had a huge impact on biomedical research, but it is one that suffers from the rule that at most three individuals can be honored. There are just too many people who have contributed to this field for the prize to be awarded without controversy.

Who most people are predicting:
Emmanuel Charpentier, Jennifer Doudna, and Feng Zhang for their discovery of CRISPR-Cas9 and its application to genome editing
Why they won't win: For this prize, it's not a matter of if they will win, but when they will win (though the prize may or may not include Zhang). Since Charpentier and Doudna's key publication in 2012, CRISPR has revolutionized biomedical science. Even if it has not yet made its way into any clinical applications, CRISPR has enabled a number of major discoveries in research and would deserve the prize just for its utility as a research tool. However, the Nobel Committee likes to wait before making its awards. The last slam-dunk prizes (discovery of RNA interference and induced pleuripotent stem cells), had to wait eight years and six years between discovery and awarding of the prize. Maybe in 2018 (six years after the key 2012 publication), I will list CRISPR as the favorite for the award.

Official prediction:
Franz-Ulrich Hartl and Arthur Horwich for their discoveries of chaperone-assisted protein folding
These two were recognized for their work in this field by a Lasker Award in 2011, which can often be a precursor to a Nobel Prize. Their major discoveries were done in the late 1980s and early 1990s and their work is a standard part of biology and biochemistry textbooks, yet it has not yet been recognized by the Nobel Committee. Unlike with epigenetics, there seems to be consensus that these two individuals deserve the credit for the key discoveries in this field. As protein misfolding plays a role in many diseases (such as Alzhemier's, Huntington's, and ALS), their work has been critical toward working to better understand and treat these conditions. The passing of Sue Lindquist, another giant in the field of protein folding, in late 2016 should hopefully serve as a reminder to the Committee to recognize this field.

Yes, this year it will most likely go to chemical biology, I think so too, but to who, what team?
 
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  • #4
  • #5
Screen Shot 2017-10-04 at 5.45.51 pm.png
Screen Shot 2017-10-04 at 5.48.46 pm.png
2017-che-laur-ill-25.jpg


2017 Nobel Prize in Chemistry
The Nobel Prize in Chemistry 2017 was awarded to Jacques Dubochet, Joachim Frank and Richard Henderson "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution".

https://www.nobelprize.org/nobel_prizes/chemistry/laureates/2017/press.html
 
  • #6
Ygggdrasil said:
Given that last year's prize for work on molecular motors was for work in the field of nanotechnology, I doubt they would make another award in the field of nanotechnology this year. However, the next time they decide to award the prize for work in nanotechnology, what discoveries and what people do you think would be worthy or honoring.

Here's my predictions (all lean towards biology as that's what I'm most familiar with):
Personal prediction (who I would want to win):
Michael Grunstein, C. David Allis, and Stuart Schreiber for their discoveries concerning the chemical modification of histone proteins in gene regulation
Why they won't win: The general field of "epigenetics" has definitely had a huge impact on biomedical research, but it is one that suffers from the rule that at most three individuals can be honored. There are just too many people who have contributed to this field for the prize to be awarded without controversy.

Who most people are predicting:
Emmanuel Charpentier, Jennifer Doudna, and Feng Zhang for their discovery of CRISPR-Cas9 and its application to genome editing
Why they won't win: For this prize, it's not a matter of if they will win, but when they will win (though the prize may or may not include Zhang). Since Charpentier and Doudna's key publication in 2012, CRISPR has revolutionized biomedical science. Even if it has not yet made its way into any clinical applications, CRISPR has enabled a number of major discoveries in research and would deserve the prize just for its utility as a research tool. However, the Nobel Committee likes to wait before making its awards. The last slam-dunk prizes (discovery of RNA interference and induced pleuripotent stem cells), had to wait eight years and six years between discovery and awarding of the prize. Maybe in 2018 (six years after the key 2012 publication), I will list CRISPR as the favorite for the award.

Official prediction:
Franz-Ulrich Hartl and Arthur Horwich for their discoveries of chaperone-assisted protein folding
These two were recognized for their work in this field by a Lasker Award in 2011, which can often be a precursor to a Nobel Prize. Their major discoveries were done in the late 1980s and early 1990s and their work is a standard part of biology and biochemistry textbooks, yet it has not yet been recognized by the Nobel Committee. Unlike with epigenetics, there seems to be consensus that these two individuals deserve the credit for the key discoveries in this field. As protein misfolding plays a role in many diseases (such as Alzhemier's, Huntington's, and ALS), their work has been critical toward working to better understand and treat these conditions. The passing of Sue Lindquist, another giant in the field of protein folding, in late 2016 should hopefully serve as a reminder to the Committee to recognize this field.

You were right. Biology it is.
But it was awarded for cryo-electron microscopy. i think your predictions were accurate, though.
 
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  • #7
Press Release: The Nobel Prize in Chemistry 2017

4 October 2017

https://www.nobelprize.org/redirect/links_out/prizeawarder.php?from=/nobel_prizes/chemistry/laureates/2017/press.html&object=kva&to=http://www.kva.se/en/ has decided to award the Nobel Prize in Chemistry 2017 to

Jacques Dubochet
University of Lausanne, Switzerland

Joachim Frank
Columbia University, New York, USA

and

Richard Henderson
MRC Laboratory of Molecular Biology, Cambridge, UK

"for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution"
Cool microscope technology revolutionises biochemistry
We may soon have detailed images of life’s complex machineries in atomic resolution. The Nobel Prize in Chemistry 2017 is awarded to Jacques Dubochet, Joachim Frank and Richard Henderson for the development of cryo-electron microscopy, which both simplifies and improves the imaging of biomolecules. This method has moved biochemistry into a new era.

A picture is a key to understanding. Scientific breakthroughs often build upon the successful visualisation of objects invisible to the human eye. However, biochemical maps have long been filled with blank spaces because the available technology has had difficulty generating images of much of life’s molecular machinery. Cryo-electron microscopy changes all of this. Researchers can now freeze biomolecules mid-movement and visualise processes they have never previously seen, which is decisive for both the basic understanding of life’s chemistry and for the development of pharmaceuticals.

Electron microscopes were long believed to only be suitable for imaging dead matter, because the powerful electron beam destroys biological material. But in 1990, Richard Henderson succeeded in using an electron microscope to generate a three-dimensional image of a protein at atomic resolution. This breakthrough proved the technology’s potential.

Joachim Frank made the technology generally applicable. Between 1975 and 1986 he developed an image processing method in which the electron microscope’s fuzzy twodimensional images are analysed and merged to reveal a sharp three-dimensional structure.

Jacques Dubochet added water to electron microscopy. Liquid water evaporates in the electron microscope’s vacuum, which makes the biomolecules collapse. In the early 1980s, Dubochet succeeded in vitrifying water – he cooled water so rapidly that it solidified in its liquid form around a biological sample, allowing the biomolecules to retain their natural shape even in a vacuum.

Following these discoveries, the electron microscope’s every nut and bolt have been optimised. The desired atomic resolution was reached in 2013, and researchers can now routinely produce three-dimensional structures of biomolecules. In the past few years, scientific literature has been filled with images of everything from proteins that cause antibiotic resistance, to the surface of the Zika virus. Biochemistry is now facing an explosive development and is all set for an exciting future.

Read more about this year's prize
https://www.nobelprize.org/nobel_prizes/chemistry/laureates/2017/popular-chemistryprize2017.pdf
Pdf 2.7 MB

https://www.nobelprize.org/nobel_prizes/chemistry/laureates/2017/advanced-chemistryprize2017.pdf
Pdf 837 Kb

To read the text you need Acrobat Reader.https://www.nobelprize.org/nobel_prizes/chemistry/laureates/2017/fig_ke_17_3Dstructures.pdf
© Johan Jarnestad/The Royal Swedish Academy of Sciences

https://www.nobelprize.org/nobel_prizes/chemistry/laureates/2017/fig_ke_en_17_blobology.pdf
© Martin Högbom/The Royal Swedish Academy of Sciences

https://www.nobelprize.org/nobel_prizes/chemistry/laureates/2017/fig_ke_en_17_dubochetspreparationmethod.pdf
© Johan Jarnestad/The Royal Swedish Academy of Sciences

https://www.nobelprize.org/nobel_prizes/chemistry/laureates/2017/fig_ke_en_17_franksimageanalysis.pdf
© Johan Jarnestad/The Royal Swedish Academy of Sciences
Jacques Dubochet, born 1942 in Aigle, Switzerland. Ph.D. 1973, University of Geneva and University of Basel, Switzerland. Honorary Professor of Biophysics, University of Lausanne, Switzerland.
https://www.nobelprize.org/nobel_prizes/chemistry/laureates/2017/www.unil.ch/dee/en/home/menuinst/people/honorary-professors/prof-jacques-dubochet.html

Joachim Frank, born 1940 in Siegen, Germany. Ph.D. 1970, Technical University of Munich, Germany. Professor of Biochemistry and Molecular Biophysics and of Biological Sciences, Columbia University, New York, USA.
http://franklab.cpmc.columbia.edu/franklab/

Richard Henderson, born 1945 in Edinburgh, Scotland. Ph.D. 1969, Cambridge University, UK. Programme Leader, MRC Laboratory of Molecular Biology, Cambridge, UK.
www2.mrc-lmb.cam.ac.uk/groups/rh15/
Prize amount: 9 million Swedish krona, to be shared equally between the Laureates.
Further information: www.kva.se and http://nobelprize.org
Press contact: Jessica Balksjö Nannini, Press Officer, phone +46 8 673 95 44, +46 70 673 96 50, jessica.balksjo@kva.se
Expert: Peter Brzezinski, member of the Nobel Committee for Chemistry, Phone +46 70-609 26 42, peterb@dbb.su.se

The Royal Swedish Academy of Sciences, founded in 1739, is an independent organisation whose overall objective is to promote the sciences and strengthen their influence in society. The Academy takes special responsibility for the natural sciences and mathematics, but endeavours to promote the exchange of ideas between various disciplines.

https://en.wikipedia.org/wiki/Cryo-electron_microscopy
 
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  • #8
Cryo-electron microscopy is very deserving and a great choice for the award. It is a technology that has enabled biologists to study the structures of many biological molecules that previously could not be obtained by other techniques like x-ray crystallography or NMR spectroscopy (two techniques that had also won various Nobel prizes).
 
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1. What is the 2017 Nobel Prize in Chemistry?

The 2017 Nobel Prize in Chemistry was awarded to Jacques Dubochet, Joachim Frank, and Richard Henderson for their work on developing cryo-electron microscopy for high-resolution imaging of biomolecules.

2. How does cryo-electron microscopy work?

Cryo-electron microscopy involves freezing samples of biomolecules in a thin layer of ice and then bombarding them with an electron beam. The resulting images are then used to create high-resolution 3D models of the biomolecules.

3. What is the significance of cryo-electron microscopy in the field of chemistry?

Cryo-electron microscopy has revolutionized the field of chemistry by allowing researchers to visualize biomolecules in their native state, providing valuable insights into their structures and functions. This technique has also opened up new possibilities for drug discovery and development.

4. How did the Nobel Prize winners contribute to the development of cryo-electron microscopy?

Jacques Dubochet, Joachim Frank, and Richard Henderson each made significant contributions to the development of cryo-electron microscopy. Dubochet discovered how to vitrify water to preserve biomolecules, Frank developed methods for image processing and 3D reconstruction, and Henderson was the first to use the technique to determine the structure of a protein at atomic resolution.

5. What other applications does cryo-electron microscopy have besides studying biomolecules?

Cryo-electron microscopy has also been used in other fields such as materials science, nanotechnology, and geology. It has also been used to study viruses and other complex biological systems, providing valuable insights into their structures and mechanisms.

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