北欧时报全程文字播报:2018年度诺贝尔化学奖公布

2018-10-03 15:34:20 来源:北欧时报

北欧时报 斯德哥尔摩报道

全程文字录入整理,翻译 /广西医科大学本科生 韦周晗

附 诺贝尔官方直播视频:https://www.youtube.com/watch?v=yc97ATQvVow&t=1010s


瑞典皇家科学院秘书Göran 宣布本年度获奖者/北欧时报



瑞典皇家科学院Sara教授解读本年度获奖者/北欧时报



Göran K. Hansson: Good morning and very welcome to the Royal Swedish Academy of Sciences. Welcome back. I should say to many of you who were here yesterday. Today we're celebrating chemistry, the academy met in session this morning, took the decision on the Nobel prize in chemistry, and we have just spoken to the new Nobel laureates. I am Jordan Hanson, I'm the secretary general of the academy, and with me today is on my right professor Claes Gustafsson who is the chairman of the Nobel committee for chemistry.

And on my left professor Sara Snogerup Linse who is a member of the committee, actually, previous chairman and an expert in the field of this year's prize. And as you shall read the announcement in Swedish and in English, and then the citation also in German, French, Russian, to cover all Alfred Nobel favorite languages, then will he remarks about the prize from Claes and an introduction to the science behind the prize by Sara. This year's prize is about harnessing the power of evolution.

The Royal Swedish Academy of Sciences has today decided to award 2018 Nobel prize in chemistry with one half to Francis H Arnold for the directed evolution of enzymes, and the other half jointly to George P Smith and Gregory P Winter for the phage display of peptides and antibodies.

And on this slide you can see some brief biographic data about our new Nobel laureates. Francis H Arnold was born in Pittsburgh, Pennsylvania, in the United States in 1956, and she's currently at the California institute of technology Caltech in Pasadena in the Los Angeles area. George P Smith was born in 1941 in Norwalk, Connecticut, uh, and he's currently at the university of Missouri in Columbia, in the United States. Sir Gregory P Winter was born in 1951 in Leicester, in the United Kingdom, and he is at the laboratory of molecular biology and the university of Cambridge in England.

So with that, I'd like to ask Claes Gustafsson, chairman of the Nobel committee to make some remarks about the prize.

Claes Gustafsson: So thank you. So this year's prize, in chemistry rewards a revolution based on evolution. Our laureates have applied principles of Darwin in the test tubes, and use this approach to develop new types of chemicals for the greatest benefit of humankind. In the natural world, evolution of proteins has been around for thousands of millions of years, all the way back until the start of life on earth.

In some mutated, proteins have evolved to improve the thickness of this life. For thousands of years, we humans have used selected reading to create animals and plants with properties that have been useful for us. This year's Nobel laureates, have taken the next step. They have used molecular understanding that we today have, of the evolutionary process and recreated a process in their laboratories in their test tubes. In doing so, they have been able to make evolution many thousand times faster.

And they have also been able to direct evolution to create proteins with new and useful properties. This work has led to the creation of proteins we knew and somatic activities able to catalyze useful chemical reactions. In addition, with a method called phage display, they've also evolved protein with proteins with new binding properties, such as antibodies that can be used to treat disease. In the laboratories, our laureates this year have been able to direct evolution, to steer it, which has led to two new chemical tools that can be used in everything from environmentally friendly, detergents to the creation of new biofuels and pharmaceuticals.

Göran K. Hansson: Thank you, Claes Sarah, can you give us some insights into the evolution of enzymes and phages?

Sara: Okay, thank you. Life on earth is the result of billions of years of evolution. Organisms have adapted our chemistry to fill in issues and environments. Random mutations in their genes lead to changes in their proteins. Many of these are enzymes. Enzymes speed up the chemical reactions in biology. Any changes that are beneficial or do no harm may be kept for the next generation, for further random cession and testing during generations to come, evolution has given us an amazing variety of creatures, full of little helpers---enzymes, chemists use enzymes to speed up reactions in their laboratories, in industrial processes and in consumer products.

Over decades, scientists have tried to improve enzymes using rational thinking. Frances Arnold realized that to really get somewhere, she needed to grasp evolution and blend in an element of randomness into the process. In 1993, she published the first example where she had used directed evolution to improve the performance of an enzyme. She took the gene from the enzyme, introduced random combinations of point mutations, expressed all these genes in bacteria that were then producing a whole library of enzyme variance. This was screened for activity, and the best variance were kept for further rounds, almost agenesis and screening until a desired level of performance was obtained. To the left, there is a model or the enzyme that she has optimized in green.

The blue is the substrate, as the diagram shows, the best variant of the free generations of random mutagenesis screening was two hundred fifty-six times better than the starting enzyme. In red, we see the side chains, the positions of the enzyme that were changed to achieve this. Nobody could have predicted this, that this particular combination who do the job. This illustrates the power of evolution and the element of randomness. Frances Arnold has since used directed evolution to improve a number of enzymes for new reaction conditions, to conduct new chemical reactions, to take in yourself straight even to make bonds for which no enzyme is available in nature. The applications are numerous and include molecules used for brain imaging, bio-fuels, pharmaceuticals, the enzymes used from directed evolution make us a good green no chemical industry where they can replace more, harsh chemical catalysts, even toxic metal ions, enzymes derived by directed evolution, also used to make high energy molecules and reaction intermediates for synthesis.

Now over to the other half of this year's Nobel prize in chemistry, where we award the phage display of peptides and antibodies. Now we get to meet a new little fellow, a bacteriophage. This is a virus that can infect bacteria. A bacteriophage is a protein capsule that in closes the DNA that codes for its own makeup. It falls the bacterium to produce new copies of the DNA and all the proteins and spit out a multiple and multitude of copies of the infecting phage.

George Smith realized that this could be used for a powerful technology. He took a foreign gene, placed it inside the gene of one of the capsule proteins, so that the encoded protein ended up on the surface of the bacteriophage. This, we call phage display. In his first work, he displayed a fragment of a protein, this we call a peptide. And he mixed the displaying phage with a million folded excess or other phages. And then he immobilized in yellow here, the antibody that's specific for this peptide, and used it to fish out the binding phages and wash out the rest.

After this, he also introduced the concept of peptide library, where he displayed not a single peptide, but the whole library of different peptides on phages. And when he used the antibody to fish, you could then get the sequences with highest affinity for the antibody and determine its epitope. To really use the technology to derive therapeutic antibodies, the phage display has to be done in reverse. Gregory Winter took a fragment of an antibody, fragment here in yellow that contains all the binding parts, and managed to display it in a fully functional form at the surface of the phage.

Again, he added a million folded excess of other phases, and he could use the target of the antibody as a fishing hook to pull it out and remove the non-binding ones. He then went on to make libraries of antibodies on phages and using an immobilized target, he could add the library, wash away the weak binding antibodies, extract the high affinity ones, and subject them to new rounds or diversification and screening to select better and better antibodies. And over just a few generations, he could obtain very high affinity and very specific antibodies.

And this forms the basis for pharmaceutical revolution. Antibodies produced by phage display are used to treat diseases such as autoimmune inflammatory diseases, anthrax and cancer, and many more are currently in clinical trials. The methods developed by Frances Arnold, George Smith, and Gregory Winter are to the highest benefit of humankind. Thank you.

Göran K. Hansson: Thank you, Sarah. I think we may now have one of our new Nobel laureates with us on the phone. Doctor Arnold, are you there?

Francis H ArnoldI am there.

Göran K. Hansson: Hello again. This is Göran Hansson. I'm the guy who woke you up in the middle of the night less than an hour ago. Have you had your cup of coffee yet?

Francis H ArnoldUm, not quite yet had this black water and my face.

Göran K. Hansson: So we are sitting now in the session hall of the Academy of Sciences, and here are nearly hundred journalists in total, and I'm sure some of them would like to ask you some questions. Are you ready for them?

Francis H ArnoldI am.

Göran K. Hansson: shall we give too much fun, had the chance to start.

SVT Reporter: Thank you. Congratulations Nobel prize.

Francis H ArnoldThank you so much.

SVT Reporter: We have had a paper here with a headline that says playing with evolution. And I was thinking maybe something similar has been said about what you did earlier. And sometimes a phrase like that could make you suspicious. What are you up to? What are you doing? Um, you have lots of questions like that. What do you usually say?

Francis H ArnoldAh, I give a factor at……(bad signal)

Göran K. Hansson: Now we have some problem with the line, I'm afraid, sorry, to interrupt, but we cannot really hear you, doctor Arnold. Uh, let's see if we can do something about it.

Francis H ArnoldThank you.

Göran K. Hansson: Ok, let's try again. So please, go ahead.

Francis H Arnold I have in that…… (bad signal)

Göran K. Hansson: Okay, what a pity! The line doesn't work. So much for sophisticated electronics. I wish they were evolutionary developed enzymes instead. Now, I don't think we get anywhere. When I give it another try, we can give it one more chance now, they have to say their questions for when you come here in December. Thank you so much for trying to with us during the press conference. And we look forward to meeting you in December when you come to receive your Nobel prize. Thank you and bye-bye.

Göran K. HanssonWell, I'm afraid you have to do with us in the panel instead the lady over there. Could you wait till you get the microphone?

Janet Wang Um, sorry, could I stand up or just sit here?

Göran K. Hansson: Just sit, please.

Janet WangOK thank you. Uh, this is Janet Wang from Nordic Chinese Times. And we notice that many of the Nobel Prizes in physics or chemistry during the decades have been awarded to the findings related to cancer, biology or physiology these years. And so my question is, um, could I ask if, um, why are these phenomena increasing this years, and what would the Nobel Prize committee suggest in the future? Thank you.

Göran K. Hansson: I think we'll ask Claes Gustafsson to comment on that.

Claes Gustafsson: There is no real intention from our side to focus on these subjects that you bring up. But it could be true if you go back to that, there could be some pattern. I think it has to do with the fact that, you know, Alfred Nobel, he wanted a prize that was for the greatest benefit of humankind. So it had to have consequences for humans. And I think that because we're always looking at both brilliant science but also brilliant science with sort of consequences. And maybe that's why you can see that some of the prizes are related to the area which you allude to.

Janet WangThank you so much. I think these findings are really inspiring and marvelous. Thank you.

Göran K. Hansson: Good to hear, good have you with us. More questions? Yes, the gentleman from associated press.

Associated Press: Thank you. So I understand that you spoke with the laureates, would you be able to tell us a little bit how they reacted? Have you mentioned speak to all of them and how was their initial reaction when you told them the good news?

Göran K. Hansson: Yes. We spoke to all three of them and they were all very happy and enthusiastic and accelerated. They look forward to coming here in December and they were also happy to share the prize with their colleagues. So it was all positive reactions. We spoke with Gregory Winter first, and then with Francis Arnold, and last with George Smith, and that they were all delighted. Yes, please.

THE JOURNALIST: I wonder if there are any patents in this field that have economic significance for pharmaceuticals or other products.

Göran K. Hansson: Sara? Would you like to answer?

Sara: Yes, Francis Arnold holds a whole range of patents. Enzymes that make bio-fuels, for example. So you can now make fossil free fuels for cars and airplanes based on her technology.

THE JOURNALIST: From what substances?

Sara: From different grown substances which is not taken out of the fossil reserves. So we knew about resources. I think she holds something like ten to fifteen patents. I am not aware the exact number. Gregory Winter also holds patents for some of the antibodies that are derived by the phage displace technology.

Göran K. Hansson: Thank you. More questions? This is your chance. Yes, please.

Green Post: Thank you. I’d like to ask you to use simple words to explain short, how significant their discoveries are.

Göran K. Hansson: I'd say very significant, but I can sort our chance to say something more.

Sara: We start with the first half. One significant is that you can now use enzymes to speed up, in principle, any reaction you want using these protocols. And you can derive enzymes that we place previous toxic catalysts in industrial processes. So I think it has a very huge significance. And the second half makes it possible to do fully human antibodies using the phage they played. These libraries are now composed of fully human lives’ antibodies from the adapted. And they can be made to be very high affinity and specificity so that you can use very small amounts in treatment.

Göran K. Hansson: So perhaps if I add safer, greener chemistry and antibody drugs with better efficiency and less side effects. More questions? Yes, please. Gentlemen over there.

THE JOURNALIST: Are there any potential damages in these researches like such as create super species could damage human kind?

Claes Gustafsson: there of course, with all sciences, there are of course risks. But when you think about the science that we talk about here, it’s sort of heavily regulated by unmodified microorganisms, or used all over the world in different labs. And we use them today to produce things like insulin, for example, treating millions and millions of people. So there is a rule-based system that is well-established and that regulates this work also. Of course, even minds can always do with things with technology. But I don't see any particular dangerous with this prize compared to many other things.

Göran K. Hansson: More questions? If not, thank you very much. And we'll close this press conference and there will be individual interviews.

THE JOURNALIST: Ms. Sara Snogerup Linse, this year's prize is for engineering proteins. Can you tell us what are proteins?

Sara: Yes, I like that question. Proteins are molecules. What a large molecule that you find everywhere in your body. They conduct almost all the processes that go on, the memory, the thinking, the calculation, the muscles. They are really the workhorse is in our bodies.

THE JOURNALIST: They are so plenty. Why to produce even more?

Sara: because in the body, some of the proteins we have or other organizers have that speed up chemical reactions. But there are reactions we want to do in chemical synthesis or to produce fuels that those enzymes can't do. So we have to improve them.

THE JOURNALIST: This is about enzymes produced by Frances Arnold this year.

Sara: That's the one half the prize. That is to make the enzymes conduct new chemical reactions or better the reactions they do today. And the other half is about improving binding proteins, these proteins that attach to something and conduct its biological processes. By this means, for example, antibodies and this technique can then be used to produce human antibodies against pathogens or other substances.

THE JOURNALIST: To come back to the main method in both prizes, so to say used, you were talking about evolution, and when we think about natural evolution, you think it's often described as a combination of chance and necessity. Is this what they did?

Sara: Yes. So this is, I would say, a combination of chance and necessity, but also quite a big element of thinking. Because what they have done is to really speed up the evolution. This nature has had billions of years, but now you want the process to be possible in maybe a few weeks or a year or something in a laboratory.

THE JOURNALIST: So it was like random experiments and then picking up the right parts of it?

Sara: Yes, I would say in nature is what a random process, because the mutations happen by chance may be due to UV radiation or something. Whereas in the laboratory it was a combination of knowledge base. You have to have some idea of which positions to vary, but then you add a random less on top of that.

THE JOURNALIST: So the biggest difference would be that you know what goals you have with while in nature. Actually there is maybe no goal.

Sara: I guess I would say nature has no goal, but what worse was and everything that makes things better or that you can populate the new getting issues then kept. Whereas in the directed evolution the scientists define the goal. I want to break this point or make this bond and I want to make it as quickly as possible at fifty-eight degrees or whatever is the condition. So the scientists define the condition.

THE JOURNALIST: And the one of the prize laureates, Frances Arnold, she knew she wanted enzymes. Why couldn't she design them from the beginning?

Sara: It's a very good question, scientists also try to do that. In principle, we know which kind of intermolecular forces operating proteins, but I think the problem is that it's a multi combinatorial problems. It's still not possible with the knowledge based message today to design an enzyme from scratch. I can design enzymes that have some catalytic efficiency, but really get somewhere, you have to bring in the power revolution to optimize them.

THE JOURNALIST: Can you tell us something about who is Francis Arnold

Sara: I think she is a is very good, very talented scientist, a very curious scientists and also goal-oriented. She knows what she wants to do, and then she sets out to do it.

THE JOURNALIST: and she made it, also the other prize, George Smith, he designed the method with this phage display, which is really hard to understand what it is. But it's a method to produce antibodies.

Sara: Yes, it's actually a method. The way he designed a method, he took those phages that are these protein capsid that have the DNA inside that codes for making the capsid. And he put into gene for the protein he wanted to study, and he then sort of full the phage to put it on its surface. So this is what we call phage display. On the top or on the bottom depending on how you turn them around. But at the tip of the phage, I think the key element of his technology that really made it fly was his physical linkage between the gene and the protein product so that you can fish out stages and then take out the DNA and work further with new generations of variations.

THE JOURNALIST: Gregory Winter used it to produce antibodies. But what is special about antibodies?

Sara: The special thing with antibodies, I mean, it’s part of our immune defense. These are proteins that nature have designed to have a possibility to become very specific. So the phage technology harness that power, antibodies have six different loops in each binding pocket that it can vary, and this is ideal, in fact, to put on a phage and a random mutagenesis to search for very high affinity antibodies. So they can have very high affinity and high specificity for a certain molecule and not react to the others.

THE JOURNALIST: And then they can be used to make drugs?

Sara: They can be use as drugs, because they can either bind to objects or surfaces we have in the body, or they can bind to things that would try to invade us.

THE JOURNALIST: How many drugs have been produced from this method?

Sara: I actually don't know, but I know that of the fifteen most sold drugs on earth, eleven of them were made by this method.

THE JOURNALIST: Are they very expensive?

Sara: I'm sure they're very expensive. But the advantage with phage display is that you can do while antibodies with such high affinity, much higher than you get to immunization, that you can lower the doses. You can use much lower doses, you can even use them containers on the skin, you don't have to inject them. So there are many advantages with them.

THE JOURNALIST: So what do you think is next was what is the vision for the future?

Sara: I think we're just at the start. I think we will see many more enzymes that catalyze bonds that we had no clue that the enzyme could actually do. One of the latest examples from Arnold’s lab or insight that catalyze the formation of carbon silicon bonds. And these are bonds you don't find in nature and there is no natural enzyme, but you managed to take one and evolve it to form these kinds of bonds that are important for making materials, for example, new materials.



公布现场/北欧时报


参考译文(广西医科大学本科生 韦周晗译)


Göran Hansson: 大家早上好,欢迎来到瑞典皇家科学院,也欢迎许多昨天到场的朋友们依旧出席今天的发布会。今天我们将揭晓诺贝尔化学奖的获奖人。今天早上的科学院会议中,我们就诺贝尔化学奖获奖者做出了决定,并且我们刚刚和新获得诺贝化学奖的获得者进行了交谈。我是学院的秘书长Göran Hansson,和我一起的是坐在我右边的诺贝尔化学委员会主席—Claes Gustafsson教授,以及坐在我左边的前任主席,今年的委员会委员Sara Snogerup Linse教授,她同时也是本次获奖领域的专家。我将宣读瑞典文和英文版的公告,以及德文、法文、俄文版的引文,以涵盖诺贝尔先生生前最喜欢的语言,之后,Claes Gustafsson将对本次获奖发表看法,Sara Snogerup Linse将介绍本次化学奖背后的机理。今年的诺贝尔化学奖是关于驾驭进化的力量。今天瑞典皇家科学会决定将2018年诺贝尔化学奖中的一半授予Francis H Arnold以表彰她首先发现酶的定向进化;另一半将由George P SmithGregory P Winter共同分享,以表彰他们在噬菌体展示技术中做出的贡献。这张幻灯片中,你可以看到一些关于新诺贝尔奖获得者的简历。Francis H Arnold1956年生于美国宾夕法尼亚州的匹兹堡,目前就职于洛杉矶帕萨迪纳的加州理工学院。George P Smith1941年生于康涅狄格州的诺沃克,目前任教于哥伦比亚的密苏里大学。Gregory P Winter爵士,1951年生于英国的莱斯特,现就职于剑桥大学分子生物学实验室。现在,我想请诺贝尔委员会主席Claes Gustafsson发表一下他的看法。

Claes Gustafsson谢谢,今年的化学奖颁给了一场基于进化论的革命。获奖者们在试管中运用了达尔文的原理,并利用这种方法开发新型化学品以求为人类带来最大利益。自然界中,蛋白质的进化已经存在了数千万年之久,甚至可追溯到地球上生命刚诞生的时候。在一些突变中,蛋白质已通过进化来改善生命的厚度。数千年以来人类一直用选择创造出对我们有用的具有某些特性的动物和植物。而今年的获奖者们,则迈出了下一步。他们利用今天分子水平上对进化的理解,在实验室中用试管重现了这一过程。而这一做法能够将进化的速度提高上千倍。通过指导进化,他们创造出新的、具有某些有用特性的蛋白质,这项工作已创造出我们已知的蛋白质以及有躯体活性的酶来催化有用的化学反应。此外,通过一种叫噬菌体展示的方法,这些噬菌体已进化出具有新结合特性的蛋白质,如可用于治疗疾病的抗体。在实验室里,今年的获奖者已经能够指导进化,引导进化,导致了两种新的化学工具的产生,可用于从环境友好的洗涤剂到创造新的生物燃料和药物等各个方面。

Göran Hansson: 谢谢你,ClaesSara,你能给我们一些关于酶和噬菌体进化的见解吗?

Sara Snogerup Linse好的,谢谢。地球上的生命是亿万年进化的结果。有机体使我们的化学反应适应了环境。有机体基因的随机突变导致它们蛋白质发生变化。这些蛋白质中大多数是酶,酶加速了生物中的化学反应,任何有益或无害的改变都将留给下一代。对于下一代将面临的进一步随机筛选和淘汰,进化给予了我们各种各样的生灵。而这一切都得益于酶,这个小小帮手。化学家利用酶来加速他们实验室中的反应,工业处理以及日用品。过去的数十年中,科学家们尝试用理性思考来改良酶。Frances Arnold意识到,若要真正有所突破,她需要掌握进化论,并在这个过程中融入随机因素。1993年,她发表了第一个模型,在这个模型中,她使用了定向进化来提高酶的性能。她从酶中提取基因,引入点突变的随机组合,在细菌中表达所有这些基因,然后产生整个酶变异文库。对活性进行筛选,并保留最佳突变以进一步循环,经培育和筛选,直到获得期望的性能水平。左边标记为绿色的是一个已最优化的模型(酶),标记蓝色的是底物。如图所示,随机突变诱变的自由世代的最佳变异体比起始酶好二百五十六倍。标记红色当中,我们可以发现,这些侧链,也就是酶的位置发生了改变来实现这一点。没人能预测到这一特定组合工作是谁做的。这也阐述了进化的力量和随机性的原理。Frances Arnold此后利用定向进化的办法改进了许多用于新反应条件的酶,进行新的化学反应,甚至可形成自然界中酶都无法利用的化学键。这项应用十分广泛,包括用于脑成像的分子、生物燃料和药物。定向进化中使用的酶可给我们带来优良的绿色、无化学物工业,用以取代更多条件苛刻的化学催化剂,甚至于有毒的金属离子。定向进化衍生的酶,也能用于制造高能分子和反应中间体以进行合成。

现在,我们来谈谈今年诺贝尔化学奖的另一半,授予了噬菌体展示所产生的肽和抗体。首先要介绍一个新的小家伙——噬菌体。噬菌体是一种能感染细菌的病毒,它由编码自身外壳的DNA以及包裹DNA的蛋白衣壳构成。它通过感染细菌来产生新的DNA及其所翻译的所有蛋白质拷贝,并吐出许多许多拷贝的感染性噬菌体。George Smith意识到这个现象可应用于强大的技术。他取出一个外源基因,把它放入其中一个编码噬菌体衣壳蛋白的基因中,这样外源基因编码的蛋白最终就出现在噬菌体的表面。我们将这一做法称为噬菌体展示。在他的第一项工作中,他展示了一个蛋白质片段,我们称之为肽。他把展示的噬菌体与一百万个折叠的噬菌体或其他噬菌体混合。然后他将肽的特异性抗体固定好,也就是图中标记为黄色的部分,并用它来钓出结合的噬菌体,并洗掉其余的噬菌体。此后,他还引入了肽库的概念。肽库中展示的不仅仅是单个肽,而是噬菌体上不同肽的整个库。当使用抗体来噬菌体这个时,可以得到抗体亲和力最高的序列,并确定其表位。若要真正利用该技术获得治疗性抗体时,必须反过来进行噬菌体展示。Gregory Winter提取了一段抗体的片段,这个片段我用黄色标记,包含所有的结合部分,并设法在噬菌体表面以全功能的形式显示出来。之后又重复一遍加入一百万个折叠的其他噬菌体的步骤,便可以将抗体的目标作为钓钩,将结合的抗体出来并筛掉不结合的抗体。然后,继续编写噬菌体上的抗体文库,并且通过固定靶,能增加文库,洗掉结合力弱的抗体,提取高亲和力抗体,并让它们接受新一轮多样化筛选,以选择更好的抗体。经过短短的几代,就可以获得亲和力很高和特异性强的抗体。上述发现和应用构成了药物革命的基石。由噬菌体展示所产生的抗体可用于治疗诸如自身免疫性炎症疾病、炭疽和癌症等疾病,还有许多抗体目前还处于临床试验阶段。由Frances Arnold George SmithGregory Winter研发的方法将为人类带来最大的效益。谢谢。

Göran Hansson: 谢谢你,Sara。我想我们可能会和一位新的诺贝尔奖获得者通话。Arnold博士,你在吗?

Francis Arnold是的我在。

Göran Hansson你好呀,我是Göran Hansson,那个不足一小时前在半夜吵醒你的家伙。有来杯咖啡吗?

Francis Arnold诶,还没准备来一杯黑色液体呢。

Göran Hansson那么我们现在坐在科学院的会议大厅里,这里差不多有近百名记者,我相信他们中的一些人想问你一些问题。你准备好了吗?

Francis Arnold是的。

Göran Hansson我们先从SVT的记者开始吧。

SVT Reporter谢谢,恭喜您获得诺贝尔奖!

Francis Arnold非常感谢。

SVT Reporter我们这儿有一篇报道的标题是与进化论玩耍。我在想,关于您之前所做的,可能也对类似的话有所耳闻。这样的短语会让你产生怀疑吗?比如你在忙什么?你在做什么?对于这样的问题,您怎么看呢?

信号故障,无法听清Arnold博士的回答。

Göran Hansson我们的电话有点问题,抱歉,打断一下,但是我们不能听见你的话,Arnold博士。呃,让我们看看我们能不能做点什么。

Francis Arnol谢谢您了。

Göran Hansson好吧,让我们再试一次。所以,请继续吧。

Göran Hansson还是不行

Göran Hansson好吧,太遗憾了!连线出问题了。对于复杂的电子产品就到此为止吧。真希望这些复杂的电子产品能是进化出的酶。我想还是不行。那我再试一次,现在我们可以再给一次机会,他们一定要问你12月份来这里的问题。非常感谢您在新闻发布会期间试着和我们连线。我们期待着在12月份你获得诺贝尔奖的时候见到你。谢谢你,再见。

Göran Hansson嗯?恐怕你得和控制台的人说而不是那边那位女士。你能等到拿到麦克风吗?

Janet Wang对不起,我该站起来呢还是坐在这儿(进行提问)?

Göran Hansson坐着就可以了。

Janet Wang好的谢谢。我是北欧时报的记者。我们留意到,这几十年来有很多诺贝尔物理学奖、化学奖都颁发给了与癌症、生物、生理学等相关的科研成果。我想问的是,为什么这种现象在这些年来有所增加呢?诺贝尔委员会对未来的科学研究有什么建议?

Claes Gustafsson从我们(诺贝尔评选委员会)的角度来说,其实并没有有意侧重于您所提及的这些学科。但如果您追溯这几十年的诺贝尔奖,这个现象有可能是真的,也有可能存在这种规律。我觉得这和阿尔弗雷德 诺贝尔的本意有关,他希望这个奖颁发给为人类带来最大贡献的人,所以这个奖必须对人类有所影响。而且我认为,我们一直都在寻找杰出的科学,也同时在找带有某种影响的杰出的科学。也许这也就是为什么您发现有些奖项与您所指的那些领域相关。

Janet Wang谢谢您!我认为,这些发现都是非常振奋人心且非同寻常的!谢谢你们!

Claes Gustafsson很高兴听到您对我们的支持!还有其他的问题么?好的,有请美联社的先生提问。

Associated Press: 谢谢您。据我了解,您有和获奖者们交谈过,那么您能告诉我他们的反应如何吗?您有提到过您曾与他们交流过吗?以及,您能说说当他们听到这一喜讯时最初的反应吗?

Göran Hansson是的,我们和他们三个人交谈过,他们都非常高兴,欣喜若狂。他们期待着12月份来到这里,也很乐意与同事分享这个奖项,都是积极反应。我们首先告知了Gregory Winter,然后是Francis Arnold,最后是George Smith,他们都很欣喜。

THE JOURNALIST: 我想知道这个领域的专利是否对药物或其他产品具有经济意义?

Sara Snogerup Linse是的,Francis Arnold拥有一系列专利。例如,制造生物燃料的酶。所以你现在可以基于她的技术为汽车和飞机生产无化石燃料。

THE JOURNALIST:从哪些物质中提取呢?

Sara Snogerup Linse根据我们对资源的了解,从种植的不同物质中,而非化石储蓄。我认为她拥有十到十五项专利。我不知道确切的数字。


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