trancekr in the wonderland

2008/10/18   Glowing Gene's Discoverer Left Out Of Nobel Prize
2008/10/10   올해 노벨 화학상 [2]
2008/07/12   과학 연구에서의 Stupidity의 중요함
2007/09/09   Selection and evolution of enzymes from a partially randomized non-catalytic scaffold

뉴비 형님 블로그에서 링크 긁어왔습니다.
진짜 연구자의 인생이란...ㅠㅠ

http://www.npr.org/templates/story/story.php?storyId=95545761

Glowing Gene's Discoverer Left Out Of Nobel Prize
by Dan Charles

Morning Edition, October 9, 2008 · The Nobel Prize in chemistry was awarded this week to three scientists working in the United States with a jellyfish protein that glows in the dark. But the scientist who found the gene for that protein, and gave it to the eventual Nobel winners, is no longer working in the field. He now drives a shuttle bus for an auto dealership.

The three chemistry Nobel Prize winners have advanced our understanding of the inner workings of cells by using the jellyfish protein to tag the tiny, intricate parts.

But to do that, back in the 1990s, those scientists first needed the gene that creates the glowing protein.

One of the winners, Roger Tsien of the University of California, San Diego, says he was lucky. At just the right time, a researcher named Douglas Prasher at the Woods Hole Oceanographic Institution in Massachusetts isolated the gene that Tsien wanted.

"So I found his phone number, called him up, and to my amazement he was willing to give out the gene," Tsien says.

Another of the Nobel laureates, Martin Chalfie of New York's Columbia University, also got the gene from Prasher.

But Prasher, it turns out, no longer works in science. He is now driving a courtesy shuttle for a car dealership in Huntsville, Ala.

"I got a hard luck story," he says.

Prasher doesn't have any regrets about giving away the gene. Tsien and Chalfie did great work, he says, which he probably couldn't have done because the National Institutes of Health had rejected his funding proposals.

"At that time, I knew I was going to get out of it; my funding had already run out," Prasher says.

He went to work for a laboratory run by the U.S. Department of Agriculture, then took a job with a NASA contractor in Huntsville. But two-and-a-half years ago, NASA cut his project and Prasher lost his job.

He tried to find a job in science but failed. So he went to work at the car dealership.

"I never thought I would enjoy working with people so much. 'Cause doing science is kind of a loner thing; but doing this, I meet new people every day, and I hear all kinds of stories, some of which I don't need to hear. Because I'm kind of a bartender," Prasher says.

But the job does not pay enough to support his family.

"Our savings is gone; just totally gone," he says.

Prasher is still looking for a research job, but he worries that after two-and-a-half years, his knowledge and skills may be out of date.

That's not what some of his former colleagues say. One called Prasher's current situation a "staggering waste of talent."

In December, Tsien and Chalfie, along with Japanese researcher Osamu Shimomura, will go to Stockholm and receive almost a half-million dollars.

Prasher says, "If they're ever in Huntsville, they need to take me out to dinner."

어찌 어찌 하다가 GFP를 공부하게 되었는데 기쁜 일이근영.
어제 랩미팅 시간에 지도 교수님도 이와 관련해서 한말씀 하셨음...ㅋㅋㅋㅋㅋㅋㅋㅋㅋ

http://nobelprize.org/nobel_prizes/chemistry/laureates/2008/press.html

Press Release

8 October 2008

The Royal Swedish Academy of Sciences has decided to award the Nobel Prize in Chemistry for 2008 jointly to

Osamu Shimomura, Marine Biological Laboratory (MBL), Woods Hole, MA, USA and Boston University Medical School, MA, USA,

Martin Chalfie, Columbia University, New York, NY, USA

and

Roger Y. Tsien, University of California, San Diego, La Jolla, CA, USA

"for the discovery and development of the green fluorescent protein, GFP".


Glowing proteins – a guiding star for biochemistry

The remarkable brightly glowing green fluorescent protein, GFP, was first observed in the beautiful jellyfish, Aequorea victoria in 1962. Since then, this protein has become one of the most important tools used in contemporary bioscience. With the aid of GFP, researchers have developed ways to watch processes that were previously invisible, such as the development of nerve cells in the brain or how cancer cells spread.

Tens of thousands of different proteins reside in a living organism, controlling important chemical processes in minute detail. If this protein machinery malfunctions, illness and disease often follow. That is why it has been imperative for bioscience to map the role of different proteins in the body.

This year's Nobel Prize in Chemistry rewards the initial discovery of GFP and a series of important developments which have led to its use as a tagging tool in bioscience. By using DNA technology, researchers can now connect GFP to other interesting, but otherwise invisible, proteins. This glowing marker allows them to watch the movements, positions and interactions of the tagged proteins.

Researchers can also follow the fate of various cells with the help of GFP: nerve cell damage during Alzheimer's disease or how insulin-producing beta cells are created in the pancreas of a growing embryo. In one spectacular experiment, researchers succeeded in tagging different nerve cells in the brain of a mouse with a kaleidoscope of colours.

The story behind the discovery of GFP is one with the three Nobel Prize Laureates in the leading roles:

Osamu Shimomura first isolated GFP from the jellyfish Aequorea victoria, which drifts with the currents off the west coast of North America. He discovered that this protein glowed bright green under ultraviolet light.

Martin Chalfie demonstrated the value of GFP as a luminous genetic tag for various biological phenomena. In one of his first experiments, he coloured six individual cells in the transparent roundworm Caenorhabditis elegans with the aid of GFP.

Roger Y. Tsien contributed to our general understanding of how GFP fluoresces. He also extended the colour palette beyond green allowing researchers to give various proteins and cells different colours. This enables scientists to follow several different biological processes at the same time.

http://www.ncbi.nlm.nih.gov/sites/entrez
http://jcs.biologists.org/cgi/content/full/121/11/1771

오랜만에 해보는 과학 관련 포스팅입니다..-.-;;;
아침에 출근했더니 지도 교수님이 실험실 애들 책상위에 한 장씩 프린트를 해서 올려놓으셨더군요.

The importance of stupidity in scientific research

Martin A. Schwartz

Department of Microbiology, UVA Health System, University of Virginia, Charlottesville, VA 22908, USA

e-mail: maschwartz@virginia.edu

Accepted 9 April 2008

I recently saw an old friend for the first time in many years. We had been Ph.D. students at the same time, both studying science, although in different areas. She later dropped out of graduate school, went to Harvard Law School and is now a senior lawyer for a major environmental organization. At some point, the conversation turned to why she had left graduate school. To my utter astonishment, she said it was because it made her feel stupid. After a couple of years of feeling stupid every day, she was ready to do something else.

I had thought of her as one of the brightest people I knew and her subsequent career supports that view. What she said bothered me. I kept thinking about it; sometime the next day, it hit me. Science makes me feel stupid too. It's just that I've gotten used to it. So used to it, in fact, that I actively seek out new opportunities to feel stupid. I wouldn't know what to do without that feeling. I even think it's supposed to be this way. Let me explain.

이어지는 내용

http://www.nature.com/nature/journal/v448/n7155/abs/nature06032.html

Letter

Nature 448, 828-831 (16 August 2007) | doi:10.1038/nature06032; Received 21 February 2007; Accepted 19 June 2007

Selection and evolution of enzymes from a partially randomized non-catalytic scaffold

Burckhard Seelig1 & Jack W. Szostak1

Howard Hughes Medical Institute, Department of Molecular Biology, and Center for Computational and Integrative Biology (CCIB), 7215 Simches Research Center, Massachusetts General Hospital, 185 Cambridge Street, Boston, Massachusetts 02114, USA
Correspondence to: Correspondence and requests for materials should be addressed to J.W.S. (Email: szostak@molbio.mgh.harvard.edu).


Enzymes are exceptional catalysts that facilitate a wide variety of reactions under mild conditions, achieving high rate-enhancements with excellent chemo-, regio- and stereoselectivities. There is considerable interest in developing new enzymes for the synthesis of chemicals and pharmaceuticals and as tools for molecular biology. Methods have been developed for modifying and improving existing enzymes through screening, selection and directed evolution. However, the design and evolution of truly novel enzymes has relied on extensive knowledge of the mechanism of the reaction. Here we show that genuinely new enzymatic activities can be created de novo without the need for prior mechanistic information by selection from a naive protein library of very high diversity, with product formation as the sole selection criterion. We used messenger RNA display, in which proteins are covalently linked to their encoding mRNA, to select for functional proteins from an in vitro translated protein library of >10¹² independent sequences without the constraints imposed by any in vivo step. This technique has been used to evolve new peptides and proteins that can bind a specific ligand, from both random-sequence libraries and libraries based on a known protein fold. We now describe the isolation of novel RNA ligases from a library that is based on a zinc finger scaffold, followed by in vitro directed evolution to further optimize these enzymes. The resulting ligases exhibit multiple turnover with rate enhancements of more than two-million-fold.