molecularbiology

123d

Austrian molecular biologist Max F. Perutz was born #OTD in 1914.

He is best known for his work on the structure of hemoglobin, for which he was awarded the Nobel Prize in Chemistry in 1962, sharing it with John Kendrew.

Using X-ray crystallography, Perutz was able to determine the three-dimensional structure of hemoglobin, which was a groundbreaking achievement in understanding how proteins function at the molecular level.

#science #molecularbiology #cristallography

1962 Press Photo Max Ferdinand Perutz co-winner Nobel Prize for Chemistry.

Max Ferdinand Perutz was born in Vienna on May 19th, 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. He was sent to school at the Theresianum, a grammar school derived from an officers academy of the days of the empress Maria Theresia, and his parents suggested that he should study law in preparation for entering the family business. However, a good schoolmaster awakened his interest in chemistry, and he had no difficulty in persuading his parents to let him study the subject of his choice.

In 1932, he entered Vienna University, where he, in his own words, “wasted five semesters in an exacting course of inorganic analysis”. His curiosity was aroused, however, by organic chemistry, and especially by a course of organic biochemistry, given by F. von Wessely, in which Sir F.G. Hopkins’ work at Cambridge was mentioned. It was here that Perutz decided that Cambridge was the place where he wanted to work for his Ph.D. thesis. With financial help from his father he became a research student at the Cavendish Laboratory in Cambridge under J.D. Bernal in September 1936, and he has stayed at Cambridge ever since.

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24d

How Colorful Ribbon Diagrams Became the Face of Proteins.

Proteins are often visualized as cascades of curled ribbons and twisted strings, which both reveal and conceal the mess of atoms that make up these impossibly complex molecules.

By Yasemin Saplakoglu via @QuantaMagazine

https://www.quantamagazine.org/how-colorful-ribbon-diagrams-became-the-face-of-proteins-20240823/

#science #molecularbiology #womeninscience

Jane Richardson’s ribbon diagrams abstract proteins’ atomic structures into beautiful, clear illustrations. In this pencil drawing of triose phosphate isomerase, alpha helices and beta strands are represented by blue spirals and green arrows, respectively.

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