cysteine

Cysteine is an important source of sulfide in human metabolism.

Cysteine is a very important molecule for a bacterium's survival.

-cysteine is also used as a processing aid for baking.

The cysteine rich protective antigen appears to play a role in this process.

In a 1994 report released by five top cigarette companies, cysteine is one of the 599 additives to cigarettes.

Throughout the length of the protein, at least every sixth residue is a cysteine.

People who lack cysteine in the hair structure are not responsive to such a curling methodology.

Experiments have shown that cysteine is also reactive to the reagent.

The most common reaction with amino acids is cysteine oxidation.

There are two other negative regulators of cysteine.

Having 6 cysteine residues, the oxidation state has a significant effect on the protein structure.

It is a derivative of the amino acid cysteine.

It contains four cysteine residues that form two disulphide bonds.

EA5 patients have a cysteine to phenylalanine mutation at position 104.

More evidence is needed to rate the effectiveness of N-acetyl cysteine for these uses.

Taking N-acetyl cysteine seems to increase the effects of nitroglycerin.

Another feature of these sequences is the conservation of cysteine residues.

The consensus pattern of cysteine conservation is shown at the bottom of Fig.

It is an intermediate in the synthesis of cysteine and adenosine.

Several conserved cysteine residues are present at positions 226,235, 335, 364,449, 581, 675, 925, and 985.

Inteins often function with the help of a catalytic cysteine.

The cysteine proteases are classified into 16 families.

The sulfite is used in essential biomolecules such as cysteine.

Some amino acids, such as cysteine and methionine contain sulfur.

The isolated cysteine rich domain folds in zinc dependent fashion.