thiol

It can also measure the number of thiol groups on proteins.

In the synthesis, a thiol is used instead of an alcohol.

Hairs with thiol groups on them slide across each other easily.

Therefore they are also sometimes referred to as thiol proteases.

The extent of thiol oxidation within the cell remains another open question.

The required thioethers can be prepared easily by exchange with a thiol.

They form in a spontaneous reaction between a thiol and an aldehyde.

The molecule contains a thiol, which is its principal site of reaction.

This reaction is similar to hydrolysis, which involves water instead of a thiol.

Activity is mediated by the two thiol groups that the molecule contains.

It acts by blocking thiol groups in the cell membranes.

The examples mentioned here illustrate the versatile potential of thiol modifications.

These reactions probably proceed via oxidative addition of the thiol.

The compound is used as a source of the thiol functional group in organic synthesis.

When the proton is taken away by a base, the thiol can become a nucleophile.

This thiol metabolite is quite different from its human equivalent, glutathione.

The thiol is area-selectively transferred to the surface based on the features of the stamp.

One of the natural amino acids, cysteine, has a thiol in its structure.

This di thiol is a useful reagent in organic synthesis.

They are the product of esterification between a carboxylic acid and a thiol.

This carboxylic acid features a pair of thiol groups.

A thioketal is first produced by reaction of the ketone with an appropriate thiol.

Mycothiol, an unusual thiol that is found in Actinobacteria.

It contains both a thiol (mercaptan) and a carboxylic acid.

In the thiol-yne reaction the substrate is a thiol.