stories of the bracket

Jane Richardson was trained as a philosopher and a physicist but soon turned to studies of protein structures. She developed a means of representing α-helices and β-sheets in tertiary structures that is now the standard for protein structures, and she has continued her work as a pioneer in protein structure study and representation. She is now a member of the National Academy of Sciences, among other awards. In honor of her beautiful illustrations that have become the standard for understanding structure/function relationships, the prize for Protein of the Year is named “The Jane Richardson Cup.”

suggested links:

http://kinemage.biochem.duke.edu/lab/richardson/richardson.php

Linus Pauling won a Nobel Prize in Chemistry in part for predicting the structures of α-helices and β-sheets in proteins. He won a second Nobel Prize in Peace for his work on nuclear disarmament and the Partial Test Ban Treaty which limited above ground nuclear testing . He was close to a third prize for the structure of DNA, but Watson and Crick beat him to it.

suggested links:

http://pauling.library.oregonstate.edu/

http://nobelprize.org/nobel_prizes/chemistry/laureates/1954/

http://nobelprize.org/nobel_prizes/peace/laureates/1962/

Dorothy Crowfoot Hodgkin was a pioneer in x-ray crystallography, and many of the early protein crystallographers credit her work as a forerunner for theirs. She solved the first structures of vitamin B12 and insulin, among other things, and she won a Nobel Prize in Chemistry for this work in 1964.

suggested links:

http://nobelprize.org/nobel_prizes/chemistry/laureates/1964/hodgkin-bio.html

Christian Anfinsen won a Nobel Prize for his elegant experiments demonstrating that the information necessary for ribonuclease folding was contained in its amino acid sequence. We know that this holds for other proteins, though sixty years later we still do a poor job of predicting a protein’s structure from its sequence.

suggested links:

http://www.nobelprize.org/nobel_prizes/chemistry/laureates/1972/anfinsen-bio.html

Max Perutz is another giant in protein x-ray crystallography, having solved the initial structures of both oxy- and deoxyhemoglobin and proposing the Perutz mechanism by which hemoglobin switches between the R state and T state to bind and release oxygen. Along with John Kendrew, he received the Nobel Prize for his work in studying the structures of globular proteins.

suggested links:

http://nobelprize.org/nobel_prizes/chemistry/laureates/1962/perutz.html