What history tells us XXV. Construction of the ribbon model of proteins (1981)The contribution of Jane Richardson

Series

DOI 10.1007/s12038-011-9110-5

What history tells usXXV.

Construction of the ribbon model of proteins (1981) The contribution of Jane Richardson

MICHEL MORANGE

Centre Cavaills, CIRPHLES USR 3308, Ecole Normale Suprieure, 29 rue dUlm, 75230 Paris Cedex 05, France

(Fax, [phone]; Email, [email protected])

following years: the design of artificial proteins and the description of the internal movements of proteins involved in their function as nanomachines. In the conclusion, I will argue that the importance of representations in scientific work is often underestimated.

2. The rise of a new representation

For protein crystallographers working at the end of the 1960s, two problems had to be addressed simultaneously.The first was to compare the different structures that were progressively revealed by X-ray crystallography, to search for resemblances between them and to classify them: to do taxonomy of proteins. The second was to find a solution to the folding problem. Following the work of Chris Anfinsen, it was widely admitted that the native state of proteins corresponded to an energy minimum. However, Cyrus Levinthal had demonstrated that this minimum could not be reached by a random search process in the range of times required for protein folding. Some rules had to guide the folding process.

Both issues were solved by considering that the association of secondary structures into super-secondary ones was the basis of protein structures, and a major step in the protein folding pathway. The first example of a super-secondary structure emerged from the work of S Rao and Michael Rossmann in 1973 on a comparison between different dehydrogenases (Rao and Rossmann 1973): a

Keywords. Protein design; protein folding; representation; ribbon model; super-secondary structure; synthetic biology

1. Introduction

In 1991, Carl-Ivar Branden and John Tooze published Introduction to protein structure (Branden and Tooze 1991): with its superb pictures and accessible text, the book quickly acquired a strong following among graduate students and newcomers to the field (Ernberg and Holmes 2004). Publication of this book was a testimony to the rapid increase of knowledge on the structure of proteins that had occurred in the 1970s. The description of protein structure had lagged behind that of DNA, and the first sausage model of myoglobin in 1957 was a deep disappointment even for John Kendrew, revealing no obvious rules of protein folding....