Nature's Robots: A History of Proteins

By Charles Tanford; Jaqueline Reynolds | Go to book overview

CHAPTER 6
Fibrous proteins

R. O. Herzog and W. Jancke found that crumpled cellulose fibres lead
to Debye-Scherrer rings in monochromatic x-rays, indicating a micro-
crystalline structure. Further x-ray results indicate that the cellulose
crystallites are oriented parallel to the fibre axis.

M. Polanyi, 1921, laying the groundwork for
all future fibre research1

It had been known for many years that not all proteins were globular proteins—that is, relatively compact, nearly spherical, charged particles. Some (like casein and gelatin) deviated grossly from this picture when studied in solution. Others, notably keratin, silk fibroin, and collagen, were not even soluble in aqueous media and could be seen in associated form under the microscope as elongated fibres. By chemical criteria, they were indubitably proteins, composed of the same amino acids as their more tractable brethren, though sometimes the proportions were unusual. Like the globular proteins, these fibrous proteins bear ionic charges. Jacinto Steinhardt, an American who had some years earlier been a postdoctoral visitor to the Carlsberg Laboratory, carried out acid– base titrations of suspensions of wool keratin, and the resulting curves were similar to those for globular proteins in solution.2


Textile fibres

In the first decades of the twentieth century, physiological interest in these fibrous proteins was almost non-existent. Compared with the oxygenbinding powers of haemoglobin or the activity of enzymes, they seemed unlikely candidates for providing insight into the meaning and mechanisms of ‘life’! On the other hand, broad semi-technical understanding of fibres was at a high level, reflecting popular interest in the subject,3 and there was a commercial motivation for investigating them—wool and silk, in particular, were important to the textile industry, which had its

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