Oral history of British science

Perutz, Max (Part 6 of 19). National Life Stories Collection: General

  • Add a note
    Log in to add a note at the bottom of this page.
  • All notes
  • My notes
  • Hide notes
Please click to leave a note

The British Library Board acknowledges the intellectual property rights of those named as contributors to this recording and the rights of those not identified.
Legal and ethical usage »

Tags (top 25):
(No tags found for this item)
  • Type


  • Duration


  • Shelf mark


  • Subjects

    Molecular Biology

  • Recording date

    2001-06-30, 2001-08-18, 2001-09-15, 2001-10-06, 2001-10-27, 2001-11-29, 2001-12-08

  • Recording locations

    Interviewee's home, Cambridge, UK

  • Interviewees

    Perutz, Max, 1914-2001 (speaker, male)

  • Interviewers

    Thompson, Katherine, (speaker, female)

  • Abstract

    Part 6: At the end of first year in Cambridge M.P. returned to Austria for a holiday, climbing mountains with his sister and friends. While there he realised that after a year in Cambridge he still had no subject for his Ph.D. He wanted a biological problem and consulted a friend in Prague, a Prof. of biochemistry -Felix Hourowitz(??) - who suggested work on structure of haemoglobin. There was a problem of getting crystals but F.H. told him that Adair(??) in Cambridge had already crystalised haemoglobin. Back in Cambridge M.P. sought an introduction to Adair(??) which materialised at a luncheon party when Adair(??) was present. Adair(??) very willingly supplied him with a tube of haemoglobin crystals which were very good and M.P. produced an excellent X-ray refraction picture. Bernal was very thrilled with it as it was only the 2nd protein crystal from which X-ray refraction pictures were taken. The first was Pepsin. Bernal had discovered that crystals had to be suspended in liquid in order to get X-ray refraction picture. He discovered that proteins were long chain of ordered molecules. It was known that chemical reactions in living cells were catalysed by proteins - the catalytic power of proteins was specific but the connection between this observation and the specific 3-dimensionl structure of protins was new. This posed the challenge: if the structure could be solved by X-ray analysis one might then understand how protein enzymes work. So this was therefore an exciting project to work with haemoglobin - M.P. explains. M.P. got horse blood from butchers and learned to extract haemoglobin. But it took 35 - 40 years to prove that horse haemoglobin had the same structure as human haemoglobin. So M.P. started his Ph.D. on haemoglobin. He showed his X-ray refraction pictures to his friends but avoided answering questions on what they meant! It was an interesting project to work on. M.P. talks about his work with Bernal on another protein - he took X-ray pictures and the results were published in Nature in March 1938, jointly with Bernal and van Kuchen(??) Work on haemoglobin showed that it existed in 2 identical halves. The X-ray picture contains only half the information - he needed to solve the structure - explains why and how to go about solving the problem. It is a complex problem for such a complicated structure.

  • Description

    Nobel Prize-winning molecular biologist and author Max Perutz is interviewed about his life and work. Mentor to James Watson, co-discoverer of DNA, Perutz died before this interview could be completed.

  • Related links

    Visit this interviewee's page on the 'Voices of Science' web resource

  • Metadata record:

    View full metadata for this item