Martin Karplus "Understanding the functioning of proteins is very important"
Martin Karplus "Understanding the functioning of proteins is very important"
Martin Karplus was born in Vienna in 1930. At the age of eight, with the suspicion that the family would produce the German occupation, he fled to the United States. He studied at Harvard College and earned a doctorate from the California Institute of Technology in 1951 under the direction of the prestigious Linus Pauling. (Pauling received two Nobel Prizes in 1954 in Chemistry and in 1962 in Peace). He has developed various methodologies of theoretical chemistry Karplus and has conducted research in many fields. He has published more than 600 articles in specialized magazines. Highlights his work in magnetic resonance. He is currently a researcher at the universities of Harvard (United States) and Louis Pasteur (France).
Karplus has offered a lecture in Donostia, by the Faculty of Chemistry of the UPV and Kutxa. Before starting the talk, Martin Karplus offered us the opportunity to chat with him, attentively.
In 1938. We left Austria before the Nazis came. My parents knew something should happen, others didn't have a chance, but we were lucky. I was eight when we went and five when I started studying English. In the family it was thought that it would be necessary and so it was. We went to Switzerland, then to France and finally to the United States.
I don't remember all the details, he was just an eight-year-old boy. But I remember sensations, trips from one side to the other and things like that.
I was not working around DNA, but with other smaller systems. But Pauling did, in that he was. In 1953 the discovery of the structure of DNA was published. Pauling was passionate about reading. She soon realized that the Watson and Crick hypothesis was correct and why she was wrong. He proposed a contrary structure (internal external and internal) and at that time appropriated his guilt.
It is true that just by reading the genome sequence we will not have a solution to genetic problems. In addition, we still do not have a complete sequence. However, it is important to take the first steps and I think this step has taught us a new way of working. Certainly, ethical problems will arise in this regard.
I did a few experiments, but they are exceptions. After leaving Pauling's laboratory, I went to England and started looking for a suitable and theoretically analyzable framework. In the end I went to the university of Illinois, because the MRI I was researching there was a new and totally appropriate field.
Proteins are non-nahi. You are also made of protein. It is therefore very important to understand how they do what they do. To do this, the system must be reviewed well. For example, when you're playing in billiards you need to analyze the direction of the ball and detect the consequence of each crash. At the same time, being proteins formed by atoms, we try to analyze the interaction of each other and understand how complete proteins move. If they were rigid systems, they could not fulfill their function, they could not catalyze reactions or carry oxygen, etc. Therefore, the movements of atoms are very important for the functioning of proteins. That's what we're modeling. But they are very large systems, with thousands of atoms.
Size is one of the difficulties. Twenty-five years ago chemists saw it impossible to model proteins, since most studied very small systems. However, it is now admitted that useful information can be extracted from these systems.
Buletina
Bidali zure helbide elektronikoa eta jaso asteroko buletina zure sarrera-ontzian