Mechanisms of Cooperativity and Allosteric Regulation in Proteins
(In this book Max Perutz, who won the Nobel Prize in 1962 ...)
In this book Max Perutz, who won the Nobel Prize in 1962 for his work on the structure of haemoglobin, shows how the functions of several allosteric proteins can be understood on the basis of their molecular mechanisms.
Glutamine Repeats and Neurodegenerative Diseases: Molecular Aspects
(This book focuses on the discovery of a common genetic ba...)
This book focuses on the discovery of a common genetic basis for a group of inherited neurological disorders, including Huntington's Disease, spino-bulbar atrophy and a series of hereditary ataxias. This shared molecular background and other similarities have led to the development of theoretical models for the pathogenesis of these diseases. It is now also clear that the mechanisms involved are likely to be of more general relevance, outside of this particular group of disorders, with implications for other neurodegenerative processes such as those involved in Alzheimer's, Parkinson's and Prion diseases. The book is an edited and updated compilation evolving from a Royal Society discussion meeting.
Is Science Necessary?: Essays on Science and Scientists
(The double-edged sword modern science wields has excited ...)
The double-edged sword modern science wields has excited controversy for years, and there is no end to the debate in sight. The genetic engineering that may one day cure cancer could also deprive the human race of its very individuality. Chemicals like DDT, which have increased food production the world over--saving millions from starvation--have also seriously polluted our environment. And most notoriously, the nuclear technology that provides us with cheap and efficient energy also fuels the horrifying weaponry of Armageddon. Such contradictions have prompted Nobel Prize-winning scientist Max F. Perutz to ask quite simply "Is science necessary?"
Throughout this provocative collection of essays--a unique blend of history, criticism, philosophy, and memoir--Perutz answers his question with a resounding "yes." Ranging from the title piece, where he examines the crucial role science has played in every aspect of modern life, to striking portraits of such great scientists as Alexander Fleming, Ernest Rutherford, Max Planck, and Chaim Weizmann, Perutz's essays demonstrate how "the survival of nature and of civilization" depends upon an intelligent and scrupulous application of science, and an understanding--by all of us--of its basic ways and means.
Some of the most compelling essays are of a personal nature. "Enemy Alien" tells the troubling story of Perutz's deportation from England as a German national during the Second World War. He provides fascinating insights into the secret military projects he worked on after the war, the most interesting of which a futuristic attempt to convert icebergs into aircraft carriers. And throughout Perutz writes of the excitement of discovery--whether of a revolutionary new medicine like penicillin or of theories such as quantum physics that forever changed the way we look at the world.
Far from being "a soulless hermit toiling away at abstruse problems that he cannot explain except in incomprehensible gibberish," the scientist, as Perutz presents him, is as impassioned as the artist, and it is from his creative energies that the most important advances in science emerge. Moving, humorous, clearly written, and, above all, enlightening, these essays help readers become aware not only of the indispensable function of science in today's world, but of the very nature of scientific inquiry itself.
Science Is Not a Quiet Life: Unravelling the Atomic Mechanism of Haemoglobin (Series in 20th Century Biology)
(Linus Pauling called haemoglobin the most interesting and...)
Linus Pauling called haemoglobin the most interesting and important of molecules. This important volume shows how X-ray crystallography was used to determine its bewilderingly complex atomic structure and to unravel the stereochemical mechanisms of its respiratory functions. It introduces isomorphous replacement with heavy atoms which led to the first protein structures, haemoglobin and its simpler relative myoglobin. Later papers deal with the stereochemistry of the cooperative effects of haemoglobin, with the relationships between the structures and impaired functions of abnormal haemoglobin, with species adaptation of haemoglobin, and with its action as a drug receptor and as an oxygen sensor. The final papers deal with amino acid repeats which act as polar zippers and their role in certain inherited neurodegenerative diseases.
Protein Structure: New Approaches to Disease and Therapy
(Dr Max Perutz, together with John Kendrew, received the 1...)
Dr Max Perutz, together with John Kendrew, received the 1962 Nobel Prize for Chemistry for using X-ray crystallography to solve the first two protein structures: haemoglobin and myoglobin. This paved the way for the solution of more than 300 protein structures that have now been determined in atomic detail. But what is the practical value of this knowledge? Has it had any effect on medical research and practice? In this volume these questions are explored by explaining how the structure of biological macromolecules is determined, and how X-ray crystallographic studies have led to new insights into disease processes and opened new approaches to medical treatment.
Max Perutz was an Austrian-born British biochemist, co-recipient of the 1962 Nobel Prize for Chemistry. He shared the award with British biochemist John C. Kendrew.
Background
Perutz was born in Vienna, Austria, on May 19, 1914. Both his parents, Hugo Perutz and Dely Goldschmidt, came from families of textile manufacturers who had made their fortune in the 19th century by the introduction of mechanical spinning and weaving into the Austrian monarchy.
Education
In 1932, Perutz entered the University of Vienna, where he studied organic chemistry till 1936. Then he landed a position as research student in the Cambridge laboratory of Desmond Bernal, who was pioneering the use of X-ray crystallography in the field of biology.
In 1940, Perutz received his doctorate at the University of Cambridge.
During the World War II the British government arrested all "enemy" aliens, including Perutz. Transported from camp to camp, Perutz ended up near Quebec, Canada, where many other scientists and intellectuals were imprisoned, including physicists Herman Bondi and Tom Gold. Always active, Perutz began a camp university, employing the resident academicians to teach courses in their specialties. It didn't take the British government long, however, to realize that they were wasting valuable intellectual resources and, by 1941, Perutz followed many of his colleagues back to his home in England and resumed his work with crystals. Perutz, however, wanted to contribute to the war effort. After repeated requests, he was assigned to work on the mysterious and improbable task of developing an aircraft carrier made of ice. The goal of this project was to tow the carrier to the middle of the Atlantic Ocean, where it would serve as a stopping post for aircrafts flying from the United States to Great Britain. Although supported both by then British Prime Minister Winston Churchill and the chief of the British Royal Navy, Lord Louis Mountbatten, the ill-fated project was terminated upon the discovery that the amount of steel needed to construct and support the ice carrier would cost more than constructing it entirely of steel.
After the war, in 1945, Perutz was finally able to devote himself entirely to pondering the smeared spots that appeared on the X-ray film of hemoglobin crystals. He returned to Cambridge, and was soon joined by John Kendrew, then a doctoral student, who began to study myoglobin, an enzyme which stores oxygen in muscles.
In 1946 Perutz and Kendrew founded the Medical Research Council Unit for Molecular Biology, and Perutz became its director. Many advances in molecular biology would take place there, including the discovery of the structure of deoxyribonucleic acid (DNA).
Over the next years, Perutz refined the X-ray crystallography technology and, in 1953, finally solved the difficult phase dilemma with a method known as isomorphous replacement. By adding atoms of mercury - which, like any heavy metal, is an excellent X-ray reflector - to each individual protein molecule, Perutz was able to change the light diffraction pattern. By comparing hemoglobin proteins with mercury attached at different places to hemoglobin without mercury, he found that he had reference points to measure phases of other hemoglobin spots. Although this discovery still required long and assiduous mathematical calculations, the development of computers hastened the process tremendously.
By 1957, Kendrew had delineated the first protein structure through crystallography, again working with myoglobin. Perutz followed two years later with a model of hemoglobin. Continuing to work on the model, Perutz and Hilary Muirhead showed that hemoglobin's reaction with oxygen involves a structural change among four subunits of the hemoglobin molecule. Specifically, the four polypeptide chains that form a tetrahedral structure of hemoglobin are rearranged in oxygenated hemoglobin. In addition to its importance to later research on the molecular mechanisms of respiratory transport by hemoglobin, this discovery led scientists to begin research on the structural changes enzymes may undergo in their interactions with various biological processes.
In 1962 Perutz left his post as director of the Unit for Molecular Biology and became chair of its laboratory.
Perutz also conducted research on hemoglobin from the blood of people with sickle-cell anemia and found that a change in the molecule's shape initiates the distortion of venous red cells into a sickle shape that reduces the cells' oxygen-carrying capacity.
Although Perutz retired in 1979, he continued to work as a professor for the MRC Lab of Molecular Biology at Cambridge and also served as a patron for the Cambridge University Scientific Society.
In his later years, Perutz was a regular reviewer for The New York Review of Books on biomedical subjects. Many of these essays are reprinted in his 1998 book I wish I had made you angry earlier.
His parents were Jewish by ancestry, but had baptised Perutz in the Catholic religion. Although Perutz rejected religion and was an atheist in his later years, he was against offending others for their religious beliefs.
Views
Quotations:
"A discovery is like falling in love and reaching the top of a mountain after a hard climb all in one, an ecstasy not induced by drugs but by the revelation of a face of nature that no one has seen before and that often turns out to be more subtle and wonderful than anyone had imagined."
"I rarely plan my research; it plans me."
"Scientists like myself merely use their gifts to show up that which already exists, and we look small compared to the artists who create works of beauty out of themselves. If a good fairy came and offered me back my youth, asking me which gifts I would rather have, those to make visible a thing which exists but which no man has ever seen before, or the genius needed to create, in a style of architecture never imagined before, the great Town Hall in which we are dining tonight, I might be tempted to choose the latter."
Membership
Perutz was elected a Fellow of the Royal Society (FRS) in 1954. He was made a Member of the German Academy of Sciences Leopoldina in 1964. He was elected to EMBO Membership in 1964.
Connections
Perutz married Gisela Clara Peiser on March 28, 1942. The couple later had a son, Robin, and a daughter, Vivian.