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The 92 pages that link to Amino acid, each with the reason it gives.

• Maillard reactionNarrower topic: Amino groups on amino acids and proteins provide key reaction partners for sugars.

• Carboxylic acidRelated: Its carboxyl group participates in peptide formation and acid–base behavior.

• EnzymeBroader topic: Their varied side chains furnish the chemical groups that perform enzyme catalysis.

• ProteinBroader topic: Proteins are assembled from amino acids joined in a specific sequence.

• Protein foldingNarrower topic: Each amino acid contributes a side chain that affects folding.

• MetabolismRelated: Amino acids supply nitrogen and carbon skeletons for biosynthesis and energy metabolism.

• Peptide bondNarrower topic: The peptide bond forms by joining functional groups on neighboring amino acids.

• Conjugate acid–base pairRelated: Its ionizable groups form conjugate acid–base pairs across physiological pH ranges.

• Origin of lifeRelated: Amino acids are among the organic building blocks investigated in prebiotic chemistry.

• Protein structureBroader topic: A protein’s primary structure is its ordered chain of amino acids.

• AlkaloidRelated: Plants and other organisms use amino acids as precursors for many alkaloid pathways.

• AbiogenesisRelated: Amino acids formed in prebiotic experiments show one route to biological building blocks.

• Transfer RNARelated: Each charged transfer RNA carries one amino acid for incorporation into a protein.

• Translation (biology)Narrower topic: These are the monomers assembled into the translation product.

• Essential amino acidNarrower topic: Essential amino acids are members of this larger molecular class.

• GlycineNarrower topic: Glycine is the smallest member of this molecular family.

• TyrosineNarrower topic: Tyrosine is one of the amino acids incorporated into proteins.

• GlucosinolatesNarrower topic: Most glucosinolate side chains are derived from amino acids or their elongated forms.

• Carboxyl groupRelated: Amino acids use their carboxyl groups in peptide-bond formation and acid–base chemistry.

• pKaRelated: Its ionizable groups have pKa values that govern charge across pH conditions.

• Active siteNarrower topic: Active-site residues contribute chemical groups that bind substrates and promote reactions.

• AlbuminNarrower topic: Albumin’s amino-acid sequence determines its folded structure and binding properties.

• Prebiotic chemistryRelated: Their formation in early-Earth simulations provides a classic test of prebiotic synthesis.

• CysteineNarrower topic: Cysteine is one of the amino acids incorporated into proteins.

• Protein engineeringBroader topic: Changing amino acids is the basic way to alter a protein's sequence.

• MonomerBroader topic: Amino acids are monomers that join to form proteins.

• Protein biosynthesisRelated: These monomers are the raw materials assembled into the protein product.

• TryptophanNarrower topic: Tryptophan is one of the 20 standard amino acids used to build proteins.

• Fischer projectionRelated: Fischer projections also represent amino-acid configurations and underpin their D–L classification.

• Miller–Urey experimentBroader topic: Several amino acids were among the products identified in the collected mixture.

• CarboxylateRelated: At common biological pH, amino acids often carry a deprotonated carboxylate group.

• Intrinsically disordered proteinBroader topic: The identities and arrangement of amino acids shape a disordered protein’s conformational preferences.

• LectinBroader topic: Amino-acid side chains help form lectin carbohydrate-binding sites.

• N-acetylcysteineNarrower topic: Cysteine belongs to this molecular family, while N-acetylcysteine is its modified derivative.

• Post-translational modificationNarrower topic: Many modifications attach to particular amino-acid side chains or protein termini.

• Weak acidRelated: Its carboxyl group commonly behaves as a weak acid in water.

• AmphoterismRelated: Its groups can accept and donate protons, giving amino acids amphoteric behavior.

• CoagulationBroader topic: Amino-acid side chains help determine how proteins respond to heat and acidity.

• GlycoproteinBroader topic: Certain amino-acid side chains provide attachment sites for protein-linked sugars.

• LysineNarrower topic: Lysine is one of the amino acids used to assemble proteins.

• Peptide hormoneNarrower topic: Peptide hormones are chains assembled from these molecular units.

• PhenylalanineNarrower topic: Phenylalanine is one of the standard amino acids used to build proteins.

• ProteolysisBroader topic: Complete proteolysis can release amino acids for reuse or metabolism.

• PeptideNarrower topic: Peptides are chains of amino acid residues linked in a specific order.

• Isoelectric pointBroader topic: Its ionizable groups provide a familiar example of charge changing with pH.

• Chemical evolutionBroader topic: Their prebiotic formation supplies candidate ingredients for early peptides.

• Proteinogenic amino acidNarrower topic: Proteinogenic amino acids are a subset defined by their incorporation into proteins.

• Alpha helixNarrower topic: Amino-acid sequence determines which helical structures a protein can form.

• Aminoacyl-tRNA synthetaseRelated: The synthetase selects one amino acid type for attachment to its tRNA.

• Beta sheetNarrower topic: Residue properties influence which sheet arrangements a sequence can adopt.