Thank you very much.
I am very glad to be here because I always enjoy very much interacting with students and young scientists,
so I hope we’ll have a lot of interaction in this conference.
I would like to start with a little historical introduction on how the ubiquitin system was discovered
because I think that it is instructive for the young people to see how or to learn how things were discovered.
And then I’ll go on to my more recent work on the roles of the system in the control of the cell division.
So I am working now or interested now for many years, more than 35 years, in the effect of how proteins in cells are degraded.
And that is a problem that interested very few people at that time when I started,
when I was about your age, a young postdoctorate fellow.
And the first slide summarises what was known about the properties of the system of intercellular protein degradation
when I started to work on it, at around 1970.
It was known that abnormal proteins, proteins that are damaged by oxidated damage or by certain mutation
are rapidly eliminated from cells by intercellular degradation.
And the take-home message that I would like you, the young students, to learn from this story,
is that when you choose a research subject, try to choose a subject that you believe it’s important
but not yet interesting to the others.
Because if it’s interesting to the mainstream, then you can be sure that the big laboratories will get there before you.
So try to do something that is not interesting to others, but you have to believe that it’s important.
And the second lesson that I would like to tell you, that biochemistry, good old-fashioned biochemistry is still very much needed.
Now we know the human genome and we know the sequence of all our genes but we don’t know,
we know the function of only about 1/3 of our genes.
And if we have genes which are only sequences of unknown function and unknown relationship to any other known enzyme,
the only way to learn how do they work is to do biochemistry,
molecular genetics is very important of course for studying function.
But without biochemistry we could never have found out such unusual mechanisms
such as targeting one protein for degradation by being linked to other proteins.
So thank you very much for your attention.
(Applause).
(WERNER ARBER) I’m pleased to be with you.
The important aspects of kinetic engineering are actually reflected man-made contributions to biological evolution.
Risks of doing so have been widely discussed and we realised rather rapidly already in the early 1970s
that a deeper insight into the Darwinian Evolution, now at the molecular level,
would be appropriate to properly evaluate risks of genetic engineering; as compared to other risks
which are and have always been in nature, namely by events of natural biological evolution.
I believed that in my genome there are only genes of importance for my own personal life, from fertilisation to my death,
I then realised that in my genome and in bacterial genomes and any other genome,
there are other genes which are not serving the purpose of that individual life but serving for biological evolution,
namely those evolution genes.
It is also clear to anybody who looks into that, that some gene products serve both purposes.
For the individual life it’s the fulfilment of that life and for the evolution genes it’s expansion of life,
that’s the source of biodiversity.
We suffer loss of biodiversity, the hope is that long term, not next year or in 10 years,
but in long term, loss of biodiversity will be reconstituted.
Not the same biodiversity, another one, but nature actually is able to propagate and produce biodiversity,
as long as living conditions exist on our planet.
With these few remarks for those medical doctors among you I like to close here.
Thank you for the attention.
(Applause).
ROBERT HUBER. I am very pleased to be in Lindau, which is a very beautiful place of my home country Bavaria,
to meet students and advertise my field of expertise, which is protein crystallography,
and perhaps convince some of you to enter this field, too.
I was very pleased to listen to Professor Blobel, the previous speaker,
who made a splendid advertisement of protein crystallography.
So I would like to continue with that.
It is a relatively young field of research, the father of it was Max Perutz, working in Cambridge, England.
But it has undergone a major transformation in the last 20 years, by the technical and methodical developments,
which originate actually in different fields, in gene technology, recombinant proteins,
high energy physics, computing and computer graphics.
Of course, all of this has, I think, reference to drug design, if you look at this as ...
proteins with drug targets, then - this is already several years old - then about 28% enzymes, of which many are proteases.
So all of these structures that I showed, or many of them, give indication of new strategies for drug design.
And I would like to add to the remarks that Sakmann made, when there is no other way,
if you would like to pursue drug development but to make a business plan.
And try to find on that basis somebody who gives money for it.
Thank you for your attention.
(Applause).
… in electro microscopy.
Now, what does it do?
... around, which is called thrombomodulin for obvious reasons.
Like active thrombin without this, what we thought obligatory proteolytic step that I showed before.
Thrombin which fundamentally changes the specificity, the activity of an enzyme, against its substrate.
So it is the first time for me to attend such a meeting as this because I have attended many meetings in many countries,
but it is about my specialised field of the science.
And this is about, most of the purpose is to get some little pieces of information about what I am doing in chemistry.
But in this meeting you not only get information about knowledge, but as well as philosophy
and also some information other than just science, so we can get to know many people from all over the country,
not only researchers but also many PhD students and so on.
Well, this is my third year in my research area, and as a young investigator
I was wondering about what other international young researchers are thinking about
and what is my identity to communicate with the society as a scientific researcher.
And I thought that this meeting would be very valuable for me to give me some answers from the valuable people,
the laureates and also from the other students, the young people from other countries.
So I decided to apply this meeting.
I think, beside the communication opportunities with the Nobel laureates and the young researchers world wide,
we can also feel the friendship of the local people and the beautiful sceneries here and that’s great.
We have face to face interview and we are selected from 20,000 people and we can come here, only 25 here in Chinese group, yeah.