Editing Max Perutz (section)

===Establishment of the Molecular Biology Unit===
After the War he returned briefly to glaciology, demonstrating how glaciers flow.<ref>{{cite journal |last=Gratzer |first=Walter |title=Max Perutz (1914–2002) |journal=Current Biology |volume=12 |issue=5 |pages=R152–R154 |date=5 March 2002 |doi=10.1016/S0960-9822(02)00727-3 |s2cid=30263181 |df=dmy-all |doi-access=free |bibcode=2002CBio...12.R152G }}</ref>

In 1947, Perutz, with the support of Professor Bragg, was successful in obtaining support from the [[Medical Research Council (United Kingdom)|Medical Research Council]] (MRC) to undertake research into the molecular structure of biological systems. This financial support allowed him to establish the Molecular Biology Unit at the Cavendish Laboratory.<ref>Medawar & Pyke. Pages 110 to 111.</ref> Perutz's new unit attracted researchers who realised that the field of molecular biology had great promise; among them were [[Francis Crick]] in 1949 and [[James D. Watson]] in 1951.

In 1953, Perutz showed that diffracted [[X-ray]]s from [[protein]] crystals could be phased by comparing the patterns from crystals of the protein with and without heavy atoms attached. In 1959 he employed this method to determine the molecular structure of the protein [[haemoglobin]], which transports [[oxygen]] in the blood.<ref name="Everts">{{cite journal|last1=Everts|first1=Sarah|title=Information Overload|journal=Distillations|date=2016|volume=2|issue=2|pages=26–33|url=https://www.sciencehistory.org/distillations/magazine/information-overload|access-date=20 March 2018}}</ref> This work resulted in his sharing with [[John Kendrew]] the 1962 [[Nobel Prize for Chemistry]]. Fifty years later, in 2013, 9,500  molecular structures of proteins were determined by X-ray crystallography.<ref name="PDB Newsletter">{{cite web |title=RCSB PDB Newsletter: Deposition & Annotation |url=https://cdn.rcsb.org/rcsb-pdb/general_information/news_publications/newsletters/2014q1/deposit.html?utm_source=chatgpt.com |website=cdn.rcsb.org |publisher=Protein Data Bank |access-date=10 February 2025 |language=en |date=Winter 2014 |issue=60}}</ref>

After 1959, Perutz and his colleagues went on to determine the structure of oxy- and deoxy- haemoglobin at high resolution. As a result, in 1970, he was at last able to suggest how it works as a molecular machine: how it switches between its deoxygenated and its oxygenated states, in turn triggering the uptake of oxygen and then its release to the muscles and other organs. Further work over the next two decades refined and corroborated the proposed mechanism. In addition Perutz studied the structural changes in a number of haemoglobin diseases and how these might affect oxygen binding. He hoped that the molecule could be made to function as a drug receptor and that it would be possible to inhibit or reverse the genetic errors such as those that occur in [[sickle cell anaemia]]. A further interest was the variation of the haemoglobin molecule from species to species to suit differing habitats and patterns of behaviour. In his final years Perutz turned to the study of changes in protein structures implicated in Huntington and other neurodegenerative diseases. He demonstrated that the onset of [[Huntington disease]] is related to the number of glutamine repeats as they bind to form what he called a "polar zipper".<ref>{{cite book |last=Perutz |first=Max |title=Science is Not a Quiet Life |chapter=1–11 |publisher=World Scientific |year=1998 |isbn=978-981-4498-51-7}}</ref>