日本語版

Ney Q-rule

concept / concept-q-rule

Qルール

Ney Q-rule is an empirical rule (Ney 1971) predicting bitterness in peptides with average hydrophobicity Q above 1400 cal/mol and molecular weight below about 6000. Later research questions its generality.

On this page (5 sections)
  1. Overview
  2. Sources for this overview (4)
  3. Topic hubs
  4. Related entries (10)
  5. Sensory (3)
↑

Reading the bitterness

The Q rule is an empirical attempt to predict whether a peptide tastes bitter from its amino-acid composition alone; it is attributed to Ney in 1971. It predicts bitterness for peptides with average hydrophobicity Q, a measure of water avoidance, above 1400 cal/mol and molecular weights of approximately 100–6000. However, only the bibliographic record of Ney's original paper has been checked for this database; the rule's content is based on its description in a citing 2008 paper.

Studies differ on how well the rule holds. A fractionation study of 2 commercial soy-protein hydrolysates stated that Q-based hydrophobicity did not support the Q rule as a predictor of bitterness. The relationship with molecular weight was not simply one-directional: bitterness peaked in fractions near 4000 or 2000, whereas fractions below 1000 were least bitter. In another study of 3 synthetic dipeptides, Gly-Phe, Gly-Leu, and Gly-Gly, the 2 more hydrophobic ones were bitter and activated hTAS2R1, whereas less hydrophobic Gly-Gly was tasteless and did not activate the receptor. This agreed with the Q rule within that range, but confirmation in only 3 dipeptides does not test the rule's generality.

A separate 2024 review quotes Ney's original formulation more fully, giving boundaries below 1300 cal/mol for non-bitter peptides and above 1400 cal/mol for bitter peptides. The range from 1300 to 1400 is not specified in the review's quotation.

A study of peptides from shrimp-head autolysate, discussed in another review, found the opposite of the Q rule's prediction: a fraction with lower average hydrophobicity had a higher bitterness score. The review says bitter components were concentrated in the 3–5 kDa fraction, and that hydrophobic amino-acid residues toward the C terminus contributed more to bitterness than those toward the N terminus.

Sources for this overview

  1. Bitter peptides activate hTAS2Rs, the human bitter receptors

    Maehashi K; Matano M; Wang H; Vo LA; Yamamoto Y; Huang L / 2008 / journal article / full text checked

    Checked for this overview: Checked the Q-rule definition and that only bibliographic information was checked for Ney's original paper. / Checked results agreeing with the Q rule for 3 synthetic dipeptides.

  2. Hydrophobicity of bitter peptides from soy protein hydrolysates

    Cho MJ; Unklesbay N; Hsieh FH; Clarke AD / 2004 / journal article / abstract checked

    Checked for this overview: Checked the result that the Q rule did not predict bitterness for soy peptides.

  3. Research on Bitter Peptides in the Field of Bioinformatics: A Comprehensive Review

    Liu S; Shi T; Yu J; Li R; Lin H; Deng K / 2024 / review / full text checked

    Checked for this overview: The 1300/1400 thresholds in Ney's original Q-rule description.

  4. Research Progress on Intelligent Prediction, Debittering Technologies, and Multi-Dimensional Evaluation for Bitter Peptides

    Wang JT; Luo C; Jiang CX; Zheng XQ / 2026 / review / full text checked

    Checked for this overview: An example in shrimp peptides in which hydrophobicity and bitterness related in the opposite direction.

Structured claims — open a section to read each claim's confidence, evidence and limits

Sensory (3)

Ney Q-rule predicts bitterness from mean hydrophobicity: A peptide with mean hydrophobicity Q > 1400 cal/mol and a molecular weight in the range of about 100-6000 is bitter (Ney's 1971 empirical rule).contested

Scope: Peptides. A prediction based solely on amino acid composition.

Note: Not supported in soy protein hydrolysates (Cho 2004, see contradicts). There is also a report of consistency at the dipeptide level (Maehashi 2008). The original Ney 1971 source was checked for bibliographic metadata only (metadata_only); the statement of the rule relies on a quotation in the full text of Maehashi 2008.

Context: "This correlation is known as the Q rule, which predicts a bitter taste for peptides with Q values higher than 1400 cal/mol and molecular weights between 100 and 6000 kDa." (verbatim)
Limitations: The original text prints the unit as "6000 kDa"; in light of the usual statement of Ney's rule (molecular weight up to 6000), this appears to be a typo for Da. The original source was not read in this survey.
Source: Bitter peptides activate hTAS2Rs, the human bitter receptors (Maehashi K; Matano M; Wang H; Vo LA; Yamamoto Y; Huang L, 2008) · full text checked
Contradicts: "The hydrophobicity data based on Q values do not support Ney's Q rule as a predictor of bitterness for soy peptides." (verbatim). Bitterness showed a nonmonotonic dependence on molecular weight, peaking at a mean molecular weight of about 4000 Da (one hydrolysate) and 2000 Da (the other), and the fraction below 1000 Da had the weakest bitterness in both hydrolysates.
Limitations: This counterevidence is limited to soy peptides. The abstract does not give the actual Q-value figures or panel size.
Source: Hydrophobicity of bitter peptides from soy protein hydrolysates (Cho MJ; Unklesbay N; Hsieh FH; Clarke AD, 2004) · abstract checked
The authors state that the result — that the hydrophobic dipeptides Gly-Phe and Gly-Leu are bitter and activate hTAS2R1, while the less hydrophobic Gly-Gly is tasteless and inactive — is consistent, at the dipeptide level, with the hypothesis linking hydrophobicity to bitterness (the Q-value rule).
Limitations: This is consistency across only 3 dipeptides, not a test of the rule's generality.
Source: Bitter peptides activate hTAS2Rs, the human bitter receptors (Maehashi K; Matano M; Wang H; Vo LA; Yamamoto Y; Huang L, 2008) · full text checked
As a method for predicting whether a peptide is bitter from its amino acid composition, the value Q is calculated from the solubility data of each amino acid; a peptide with Q < 1300 is not bitter, and a peptide with Q > 1400 shows bitterness, the source states.
Limitations: Only the summary was checked. The summary does not specify how the intermediate band of 1300-1400 is treated.
Show dataconcept-q-rule —predicts_bitterness_from_mean_hydrophobicity→ "A peptide with mean hydrophobicity Q > 1400 cal/mol and a molecular weight in the range of about 100-6000 is bitter (Ney's 1971 empirical rule)."
claim: clm-q-rule-bitterness-prediction / type: sensory / updated: 2026-08-30
Ney Q-rule is defined as In Ney's (1971) original statement of the Q-value rule (Ney's rule), a peptide with a Q-value below 1300 cal/mol is not bitter and a peptide above 1400 cal/mol is bitter; the range of 1300-1400 is not specified.contextual

Scope: Layer: literature. A statement in a 2024 review that cites the original Ney 1971 source.

"In 1971, Ney et al. proposed the Q rule, primarily used to describe and predict the bitterness level of peptides by calculating the frequency of hydrophobic amino acid residues to obtain a Q value. Peptides with a Q value less than 1300 are not bitter, while those with a Q value greater than 1400 are bitter."
Limitations: The original Ney 1971 source (a German-language paper) was not checked by this team; this relies on the summary given in the 2024 review.
Source: Research on Bitter Peptides in the Field of Bioinformatics: A Comprehensive Review (Liu S; Shi T; Yu J; Li R; Lin H; Deng K, 2024) · full text checked
Show dataconcept-q-rule —is_defined_as→ "In Ney's (1971) original statement of the Q-value rule (Ney's rule), a peptide with a Q-value below 1300 cal/mol is not bitter and a peptide above 1400 cal/mol is bitter; the range of 1300-1400 is not specified."
claim: clm-w71d1-q-rule-original-thresholds / type: sensory / updated: 2026-09-07
Ney Q-rule does not predict A study examining peptides derived from the autolysis products of shrimp heads reports that the fraction with lower mean hydrophobicity showed, conversely, stronger bitterness; the bitter components were concentrated in the 3-5 kDa molecular weight fraction; and hydrophobic amino acid residues at the C-terminus contributed more strongly to bitterness than those at the N-terminus.preliminary

Scope: Layer: literature (secondary citation). A study of shrimp-head autolysate peptides by Fu et al. (original not read), as summarized by the Wang et al. 2026 review.

Note: Secondary citation. The original (Fu et al.) was not checked; this is based on the summary statement in Section 2.1 of Wang et al. 2026 (Foods, full text checked).

"Fu et al. used the self-digestion product of shrimp heads as the research model...they found that the core bitter components in the hydrolysis products were mainly concentrated in the peptide segments of 3-5 kDa. Among the different molecular weight components separated, the components with a lower average hydrophobic value actually showed stronger bitterness. Moreover, the positioning of the hydrophobic amino acid residues at the N-terminal or C-terminal of the peptide chain determines their bitter properties, and the bitter response caused by the C-terminal residues is significantly stronger than that of the N-terminal residues."
Limitations: The original (Fu et al.) was not checked by this team; this relies on the summary given by the 2026 review (secondary citation).
Show dataconcept-q-rule —does_not_predict→ "A study examining peptides derived from the autolysis products of shrimp heads reports that the fraction with lower mean hydrophobicity showed, conversely, stronger bitterness; the bitter components were concentrated in the 3-5 kDa molecular weight fraction; and hydrophobic amino acid residues at the C-terminus contributed more strongly to bitterness than those at the N-terminus."
claim: clm-w71d1-q-rule-shrimp-counterexample / type: sensory / updated: 2026-09-07

↑ Top of page · ← Encyclopedia (English entries)