Related Experiment Video
Updated: Jun 2, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
Published on: November 30, 2018
Are structural proteins in insect cuticles dominated by intrinsically disordered regions?
1The Collstrop Foundation, The Royal Danish Academy of Sciences and Letters, H.C. Andersens Boulevard 35, 1553 Copenhagen V, Denmark. soa@royalacademy.dk
Abstract:
Fifty years ago it was concluded that the highly elastic cuticular protein, resilin, is devoid of secondary structure and that the peptide chains are randomly coiled and easily and reversibly deformed. These properties indicate that resilin is an intrinsically disordered protein and suggest that also other cuticular proteins may contain disordered regions. Amino acid sequences are now available for cuticular proteins from many insect species, and several programs have been developed to predict the probability for a given protein to contain disordered regions. The present paper describes the results obtained when the predictors are applied to various types of cuticular proteins from several insects. The results suggest that most cuticular proteins contain shorter or longer disordered regions, and the possible functions for such regions are briefly discussed.
More Related Videos
Related Concept Videos
Intrinsically Disordered Proteins
Intrinsically Disordered Proteins
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
Fibrous Proteins
Structural Protein Function
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
Structural Protein Function
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...

