Insulin Fibril Model
based on LVEALYL Peptide Crystal Structure
Summary: LVEALYL and LYQLEN segements form the core of the fibril.
Each successive strand in the spine is translated
by 4.74 Angstroms and rotated by -0.7 degrees.
The pitch is 2398 Angstroms.
The average radius is 50 Angstroms.
Current view: Insulin A chains (red) containing the segment LYQLEN are on the outside of the fibril.
Insulin B chains (blue and purple) containing the segment LVEALYL are on the inside of the fibril. Disulfide bonds are shown in yellow.
To show in space filling mode, push button.
1) Four parallel beta sheets compose the spine of the fiber. To return to a cartoon representation, push the button.
2) The steric zipper side chains are shown in green.
The sheets are held together by Van der Waals forces, and a tight steric fit that excludes water molecules.
3) The asymmetric unit of the fibril is composed of two insulin molecules, shown here.
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