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Protein Glossary

Glossary

Plain-English definitions of the protein science terms you’ll see across ProteinMD.

Amino acids
The 20 building blocks of protein. Nine are essential: your body can’t make them, so they must come from food.
Anabolic resistance
The blunted muscle-building response to protein seen with aging, inactivity or illness, and a reason seniors need more protein per meal.
Anabolic window
The period after exercise when muscles are especially responsive to protein. Practically: eat 20–40 g of quality protein within about 2 hours of training.
Anti-nutrients
Compounds such as phytates, lectins and trypsin inhibitors in some plant foods that reduce protein or mineral absorption. Soaking, sprouting, fermenting and cooking reduce them.
BCAAs
Branched-chain amino acids: leucine, isoleucine and valine.
Bioavailability
How much of a nutrient is digested, absorbed and used by the body. For protein it depends on digestibility and amino acid profile.
Casein
The slow-digesting milk protein (~80% of milk protein). Forms a gel in the stomach and releases amino acids for hours, ideal before sleep.
CKD & eGFR
Chronic kidney disease is staged by eGFR (estimated glomerular filtration rate). Stages 3–5 not on dialysis usually call for reduced protein (0.55–0.6 g/kg per KDOQI 2020).
Collagen
Structural protein rich in glycine and proline but lacking tryptophan, so it is not a complete protein and scores 0 on PDCAAS.
Complementary proteins
Two proteins whose limiting amino acids differ, so eating them together (or across the day) forms a complete profile, like rice and beans.
Complete protein
A protein that supplies all nine essential amino acids in adequate proportions, e.g. eggs, dairy, meat, fish, soy, quinoa and mycoprotein.
DIAAS
Digestible Indispensable Amino Acid Score. The FAO’s preferred method (2013) that measures digestibility of each amino acid at the end of the small intestine. Not capped: ≥100% excellent, 75–99% high, <75% no quality claim.
Essential amino acids (EAAs)
Histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan and valine.
g/kg
Grams of protein per kilogram of body weight per day, the standard way to express protein needs. 1 kg = 2.2 lb.
Leucine
A branched-chain essential amino acid that acts as the main trigger for muscle protein synthesis via mTOR.
Leucine threshold
The ~2.5–3 g of leucine per meal needed to maximally stimulate muscle protein synthesis in adults. Older adults may need slightly more.
Limiting amino acid
The essential amino acid in shortest supply relative to need. It caps how much of that protein your body can use. Legumes are usually limited in methionine; grains, nuts and seeds in lysine.
MPS (muscle protein synthesis)
The process of building new muscle proteins. Stimulated by protein intake (especially leucine) and resistance exercise.
mTOR
Mechanistic target of rapamycin, a cellular signaling hub that switches on protein synthesis when it senses leucine, insulin and mechanical load.
Mycoprotein
Protein from the fungus Fusarium venenatum (e.g. Quorn). A complete, high-fiber meat alternative.
Nitrogen balance
The difference between nitrogen eaten (from protein) and excreted. Positive balance means net protein gain, e.g. during growth or muscle building.
PDCAAS
Protein Digestibility-Corrected Amino Acid Score. Rates protein quality from 0 to 1.0 using overall (fecal) digestibility. Capped at 1.0, so top-quality proteins look identical.
PKU (phenylketonuria)
An inherited disorder in which the body can’t break down phenylalanine. Managed with a Phe-restricted diet and Phe-free protein substitutes.
RDA
Recommended Dietary Allowance: 0.8 g/kg/day for adults. A minimum to prevent deficiency, not an optimal target for active people.
Sarcopenia
Age-related loss of muscle mass and strength. Adequate protein (1.0–1.2 g/kg for adults 65+) and resistance training help prevent it.
Whey
The fast-digesting milk protein (~20% of milk protein). Very high in leucine; popular post-workout.

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