Related Experiment Video
Updated: Jul 14, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Structure of cholesterol helical ribbons and self-assembling biological springs
Boris Khaykovich1, Chintan Hossain, Jennifer J McManus
1Nuclear Reactor Laboratory, Massachusetts Institute of Technology, 138 Albany Street, Cambridge, MA 02139, USA.
Abstract:
We report the results of x-ray-scattering studies of individual helical ribbons formed in multicomponent solutions of cholesterol solubilized by various surfactants. The solutions were chemically defined lipid concentrate (CDLC) and model bile. In these and many analogous multicomponent surfactant-cholesterol solutions, helical ribbons of two well defined pitch angles, namely 11 degrees and 54 degrees, are formed. We have suggested previously that this remarkable stability results from an underlying crystalline structure of the sterol ribbon strips. Using a synchrotron x-ray source, we have indeed observed Bragg reflections from individual ribbons having 11 degrees pitch angle. We have been able to deduce the parameters of the unit cell. The crystal structure of these ribbons is similar to that of cholesterol monohydrate, with the important difference that the length of the unit cell perpendicular to the cholesterol layers is tripled. We discuss possible origins for this triplication as well as the connection between the crystalline structure and the geometrical form of the helical ribbons.
Related Concept Videos
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein Organization
Protein Organization
The primary structure of a protein is its amino acid sequence.
Assembly of Cytoskeletal Filaments

