Related Experiment Video
Updated: Aug 13, 2026

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism
Published on: December 18, 2013
Secondary structures and conformational changes in flagelliform, cylindrical, major, and minor ampullate silk
Cedric Dicko1, David Knight, John M Kenney
1Department of Zoology, Oxford University, Oxford OX1 3PS, United Kingdom. cedric.dicko@zoology.ox.ac.uk
Abstract:
Orb weaver spiders use exceptionally complex spinning processes to transform soluble silk proteins into solid fibers with specific functions and mechanical properties. In this study, to understand the nature of this transformation we investigated the structural changes of the soluble silk proteins from the major ampullate gland (web radial threads and spider safety line); flagelliform gland (web sticky spiral threads); minor ampullate gland (web auxiliary spiral threads); and cylindrical gland (egg sac silk). Using circular dichroism, we elucidated (i) the different structures and folds for the various silk proteins; (ii) irreversible temperature-induced transitions of the various silk structures toward beta-sheet-rich final states; and (iii) the role of protein concentration in silk storage and transport. We discuss the implication of these results in the spinning process and a possible mechanism for temperature-induced beta-sheet formation.
Related Concept Videos
Protein Folding
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
Studying the Cytoskeleton
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Flagella and Motility in Bacteria
Bacterial Protein Maturation

