The two resulting chains are kept together by a disulfide bond.

When two sulfur atoms come together, they form what is called a disulfide bond.

Like other type 2 cystatins, it has two disulfide bonds.

In order to analyze the structure of proteins, it is often necessary to break disulfide bonds.

Some family members have an additional disulfide bond also in a conserved location.

The molecule is folded due to the activity of three disulfide bonds.

This is important for the different helices to form tight disulfide bonds.

In this time disulfide bonds will be broken by the released cyanide.

Naturally curly hair has a lot of disulfide bonds.

Cysteine is excluded because of its liability to form disulfide bonds.

These two regions are linked by two or three disulfide bonds.

It contains three disulfide bonds and a total of four possible glycosylation sites.

Each module contains two small beta sheets and three disulfide bonds.

Disulfide bonds decrease the free energy of the open state compared to the closed state.

Additional work suggests that it plays a role in resolving mixed disulfide bonds.

Specifically, they act to "reduce" disulfide bonds between hair amino acids.

It can be a separate unit that is attached to the rest of the receptor by a disulfide bond.

Important to the discussion of disulfide bond formation is the order in which disulfides are formed.

The disulfide bonds give hair its elasticity, and can be reformed with chemicals.

The subunits are linked by a single covalent disulfide bond.

This may account for its need of four disulfide bonds to stabilize its structure.

These proteins are characterized by having three disulfide bonds in a characteristic motif.

The single species with no disulfide bonds is usually denoted as R for "fully reduced".

The new disulfide bonds keep the hair curling the way it was set.)

It is hypothesized that the two monomers are held together via disulfide bonds.