Dorothy Hodgkin e seus estudos cristalográficos sobre a estrutura da penicilina

ResumoDorothy Crowfoot Hodgkin formou-se em química pela Somerville Oxford, doutorou-se em Cambridge e liderou o grupo de pesquisa que decifrou a estrutura molecular de várias moléculas biológicas complexas como: a penicilina, a vitamina B12 e a insulina. Seu nome não foi tão ovacionado quanto o de outros ganhadores do Prêmio Nobel já que seu método de trabalho, a cristalografia de raio X para a análise de moléculas complexas era ainda pioneiro e pouco disseminado entre os laboratórios da época. Foi a busca de soluções exatas para problemas difíceis que motivaram Dorothy a superar tempos de guerra, contratempos experimentais, demandas do casamento, da maternidade e a dor física persistente, para se tornar uma das maiores cientistas do século. Neste trabalho apresentaremos brevemente a vida de Dorothy, sua infância distante dos pais e rica em experiências culturais, sua juventude, as dificuldades que precederam sua entrada na Universidade e sua vida como pesquisadora, e mais especificamente, falaremos sobre sua colaboração para a solução da estrutura molecular da penicilina no cenário da Segunda Guerra Mundial. Nosso objetivo é apresentar ao leitor o trabalho de Dorothy ancorados em suas publicações originais e suas biografias, de maneira a contribuir com a disseminação da história das mulheres na ciência. Palavras-chave: Dorothy Crowfoot Hodgkin; Penicilina; Mulheres na Ciência.AbstractDorothy Crowfoot Hodgkin graduated in chemistry from Somerville Oxford, doctorate from Cambridge and led the research group that deciphered the molecular structure of several complex biological molecules such as penicillin, vitamin B12 and insulin. Her name was not as ovation as that of other Nobel Prize winners since their method of working, X-ray crystallography for the analysis of complex molecules was still pioneering and little disseminated among laboratories of the time. It was the search for exact solutions to difficult problems that motivated Dorothy to overcome wartime, experimental setbacks, marriage demands, maternity, and persistent physical pain to become one of the greatest scientists of the century. In this work we will briefly present the life of Dorothy, her childhood far from her parents and rich in cultural experiences, her youth and the difficulties that preceded her entrance into the University and her life as a researcher, and more specifically, we will talk about her collaboration for the solution of molecular structure of penicillin in the scene of World War II. Our goal is to present the Doroty works, anchored in her original published and her biographies in order to contribute with the dissemination of history of women in science.Keywords: Dorothy Crowfoot Hodgkin; Penicillin; Women in Science.

Protein Crystallography: Getting in on the Ground Floor

The first diffraction pattern from crystals of a protein was obtained by Desmond Bernal and Dorothy Crowfoot Hodgkin in 1934. As early as 1939, Bernal described how such diffraction patterns might be used to determine the complete three-dimensional structure of a protein. It was not until 1954, however, that Max Perutz showed how isomorphous replacement could be used to determine the phases for crystalline hemoglobin. Using this approach, Kendrew and coworkers described the three-dimensional structure of myoglobin in 1960. In 1965, David Phillips' group determined the structure of hen egg-white lysozyme. Then, in 1967, three different protein crystal structures were reported. Macromolecular crystallography had come of age. The talk will touch on some of these early events and include reminiscences of work at the MRC Lab in David Blow's group leading up to the successful determination of the alpha-chymotrypsin structure.