These form three disulphide bonds, which are required for activity.

The monomers are held together by 2 interchain disulphide bonds.

All have four conserved cysteines that probably form two disulphide bonds.

Colipase is a small protein with five conserved disulphide bonds.

It contains four cysteine residues that form two disulphide bonds.

Proteins with disulphide bonds and glycosylation can be efficiently produced in yeast.

The two disulphide bonds are as predicted.

This domain contains four conserved cysteines involved in two disulphide bonds.

There are two disulphide bonds in pelC and 12 proline residues.

Alternatively, these cysteine residues could participate in intermolecular disulphide bonds.

They have a compact, globular fold (similar to other interleukins), stabilised by the 2 disulphide bonds.

'C': conserved cysteine involved in a disulphide bond.

This fold, and the location of the disulphide bonds, are a shared element between toxins stemming from arthropods.

Fourteen cysteines are conserved in all known HER-1 sequences and form seven disulphide bonds.

They are also termed S-type lectins due to their dependency on disulphide bonds for stability and carbohydrate binding.

E. disulphide bond) is a covalent bond, usually derived by the coupling of two thiol groups.

Around 35 to 40% of the residues are conserved in both proteins as well as the positions of the four disulphide bonds.

The cysteine side chains connect the beta-sheet and the helix via disulphide bonds to form the core of the molecule.

The collagen IV C4 domain contains 12 cysteines, and all of them are involved in disulphide bonds.

LEAP2 contains a core structure with two disulphide bonds formed by cysteine residues in relative 1-3 and 2-4 positions.

Additionally cathelicidins may also be small-sized molecules (12-18 residues) with beta-hairpin structures, stabilized by one or two disulphide bonds.

In structure, IL-10 is a protein of about 160 amino acids that contains four conserved cysteines involved in disulphide bonds.

The EMI domain possesses six highly conserved cysteine residues, which likely form disulphide bonds.

Oxidizing conditions like HO cause disulphide bonds to form in Hsp33, a process that leads to the activation of its chaperone function.

To form the mature insulin, the proinsulin is then cleaved at two positions to yield two polypeptide chains linked by 2 disulphide bonds.