nutrient

Cysteine

A sulfur-containing amino acid whose side chain can form disulfide bonds.

Educational draft · Human scientific and editorial review pending. About review status

Cysteine contributes sulfur to proteins and to oxidation–reduction chemistry.

How it works

A bond that can stabilise proteins

Two cysteine side chains can join to form a disulfide bond, helping stabilise selected folded proteins.

Related topics

Worth knowing

  • It is linked to methionine metabolism. Methionine and cysteine are the principal sulfur-containing amino acids.

A closer look

Its sulfur changes with redox conditions

The thiol group can switch between reduced and oxidised forms, so cysteine chemistry depends on its local redox environment.

Redox state matters

The thiol group can switch between reduced and oxidised forms, so cysteine chemistry depends on the local redox environment.

References

Source-checked local draft.
Human editorial review pending.

  1. NIH National Library of Medicine (opens in new tab)Biochemistry, Essential Amino AcidsChecked 2026-09-05
  2. NIH National Library of Medicine (opens in new tab)Biochemistry, Protein CatabolismChecked 2026-09-05
  3. NIH National Library of Medicine (opens in new tab)Biochemistry, Primary Protein StructureChecked 2026-09-05
  4. NIH National Library of Medicine (opens in new tab)Biochemistry, Collagen SynthesisChecked 2026-09-05