nutrient
Proline
An amino acid whose ring structure changes the shape of protein chains.
Educational draft · Human scientific and editorial review pending. About review status
Proline is common in collagen and can introduce bends into protein backbones. The body can also synthesise it.
How it works
A ring that bends the chain
Proline’s side chain loops back to its amino nitrogen, restricting the chain’s geometry and often introducing a bend in an alpha helix.
Related topics
Proline is used to build Protein
Proline is one of the amino acids used to assemble proteins.
Evidence: Established · Source checked 2026-09-05 · Sources: NIH National Library of Medicine: Biochemistry, Essential Amino Acids
Worth knowing
It is common in collagen. Proline and hydroxyproline are abundant in collagen and help shape its triple helix.
A closer look
Some residues are hydroxylated
During collagen synthesis, selected proline residues are hydroxylated after translation; the modified residues help stabilise the collagen helix.
Hydroxyproline is a modified residue
Collagen synthesis modifies selected proline residues after translation, changing the stability of the collagen helix.
References
Source-checked local draft.
Human editorial review pending.
- NIH National Library of Medicine (opens in new tab)Biochemistry, Essential Amino AcidsChecked 2026-09-05
- NIH National Library of Medicine (opens in new tab)Biochemistry, Protein CatabolismChecked 2026-09-05
- NIH National Library of Medicine (opens in new tab)Biochemistry, Primary Protein StructureChecked 2026-09-05
- NIH National Library of Medicine (opens in new tab)Biochemistry, Collagen SynthesisChecked 2026-09-05
Take it into the kitchen
Explore this nutrient in simple meals. Recipe pages show estimated amounts and missing data.
Chicken corn tortilla fold · 20 min →
Tomato aubergine mozzarella pasta · 25 min →
Pineapple cottage cheese bowl · 10 min →
Compare meals by proline →