scleroprotein

A scleroprotein occurs as an aggregate due to hydrophobic side chains that protrude from the molecule.

Scleroprotein are structural proteins or storage proteins that are typically inert and water-insoluble.

Scleroprotein is a simple protein found in horny and cartilaginous tissues and in the lens of the eye.

A scleroprotein's peptide sequence often has limited residues with repeats; these can form unusual secondary structures, such as a collagen helix.

Another use of NMO is in the dissolution of scleroprotein (found in animal tissue).

David Anthony Dougall Parry, CNZM is a renowned New Zealand biophysicist known for his work within the area of ultrastructure scleroprotein analysis.

Type-III collagen is a fibrous scleroprotein in bone, cartilage, dentin, tendon, bone marrow stroma and other connective tissue; yields gelatin on boiling.

Typically, palynomorphs are dinoflagellate cysts, acritarchs, spores, pollen, fungi, scolecodonts (scleroprotein teeth, jaws and associated features of polychaete annelid) worms, arthropod organs (such as insect-mouth parts), chitinozoans and microforams.

There is a steady increase in the elastin content of the lamina propria as we age (elastin is a yellow scleroprotein, the essential constituent of the elastic connective tissue) resulting in a decrease in the ability of the lamina propria to expand caused by cross-branching of the elastin fibers.