Pronunciation: [mˈaks pˈɛɹʌts] (IPA) 
Max Perutz was an Austrian-born British molecular biologist who shared the Nobel Prize in Chemistry in 1962. His name is pronounced as "mæks ˈpɛrʊts" in IPA phonetic transcription. The first name "Max" is pronounced as "mæks" with the 'a' sound in "cat" and a short 's' sound. The last name "Perutz" is pronounced as "ˈpɛrʊts" with a stress on the first syllable, a short 'e' sound, and a silent 'z' sound at the end.
Max Perutz was an Austrian-born British molecular biologist and Nobel laureate, widely recognized for his pioneering contributions in the field of protein structure determination using X-ray crystallography. Born on May 19, 1914, in Vienna, Austria, Perutz fled to England in 1936 due to the rising threat of Nazi Germany. He completed his Ph.D. in Chemistry at the University of Cambridge and later became a prominent member of the scientific community.
Perutz's seminal work focused on unlocking the three-dimensional structures of proteins, primarily hemoglobin – the molecule responsible for oxygen transport in red blood cells. He collaborated extensively with other distinguished scientists, such as John Kendrew, to develop and refine X-ray diffraction techniques to unravel these complex structures.
His findings not only provided crucial insights into the structure-function relationship of proteins but also laid the foundation for understanding diseases related to protein misfolding, such as sickle cell anemia. Moreover, Perutz's studies paved the way for the field of structural biology and contributed significantly to advancements in drug design and development.
Max Perutz was awarded the Nobel Prize in Chemistry in 1962, jointly with Kendrew, for "their studies of the structures of globular proteins." He received numerous accolades throughout his career, including the Copley Medal and the Royal Medal of the Royal Society, among others.
Max Perutz's remarkable achievements continue to inspire generations of scientists, cementing his status as one of the foremost pioneers in protein crystallography and contributing immensely to our understanding of the molecular world.
