Peptide bond

Definition

In organic chemistry, a peptide bond is an amide type of covalent chemical bond linking two consecutive alpha-amino acids from C1 of one alpha-amino acid and N2 of another, along a peptide or protein chain.

Related concepts

ADP-ribosylation Acetylation Activation energy Acylation Adenosine triphosphate Adenylylation Agostic interaction Alanine Allysine Alpha-amanitin Alpha-amino acid Amide Amine Amino Amino acid Amino group Antiperiplanar Arginine Aromaticity Asparagine Aspartate Aurophilicity Baird's rule Bent bond Bicycloaromaticity Bond cleavage Butyrylation C terminus Calorie Carbamylation Carbon Carbonyl Carboxyl group Carboxylation Carboxylic acid Catalysis Cation–pi interaction Chalcogen bond Charge-shift bond Chemical bond Cis-trans isomerism Citrullination Condensation reaction Conjugated system Coordinate covalent bond Covalent bond Cyclol Cysteine C–H···O interaction Deamidation Deamination Dehydration reaction Dehydration synthesis Dephosphorylation Desmosine Detyrosination Dihedral angle Dihydrogen bond Dipeptide Diphthamide Disulfide bond Eight-center two-electron bond Electron counting Electron deficiency Electronegativity Enzyme Ester Flavin group Formylation Four-center two-electron bond Functional group Gibbs energy Glutamate Glutamate–cysteine ligase Glutamine Glutarylation Glutathione Glutathione synthetase Glycation Glycine Glycophosphatidylinositol Glycosylation Green Fluorescent Protein Half life Halogen bond Hapticity Heterolysis (chemistry)Histidine Histidine ammonia-lyase Homoaromaticity Homolysis (chemistry)Hydrogen Hydrogen bond Hydrolysis Hydroxyl Hydroxylation Hydroxylysine Hyperconjugation Hypervalent molecule Hückel's rule Imine Intein Intercalation (chemistry)Intermolecular force Intramolecular force Ionic bonding Isopeptide bond Jemmis mno rules Joule Kaede (protein)Lactylation London dispersion force Lone pair Low-barrier hydrogen bond Lysine Lysine malonylation Lysine methylmalonylation Lysine tyrosylquinone Mechanically interlocked molecular architectures Metal aromaticity Metallic bonding Metallophilic interaction Metal–ligand multiple bond Methionine Methylation Mole (unit)Myristoylation Möbius aromaticity N terminus Nitrogen Non-covalent interactions Nonribosomal peptide N–O acyl shift O-GlcNAc O-glycosylation O-methylation Organic chemistry Oxygen Palmitoylation Peptide Phosphorylation Pi backbonding Plane (geometry)Polyglutamylation Polyglycylation Polyhedral skeletal electron pair theory Porphyrin Posttranslational modification Prenylation Proline Propionylation Protease Protein Protein acetylation Protein biosynthesis Protein folding Protein primary structure Proteolysis Racemization Resonance-assisted hydrogen bond Ribosome SUMO protein Salt bridge (protein and supramolecular)Serine Side chain Spherical aromaticity Stacking (chemistry)Succinylation Sulfilimine bond Symmetric hydrogen bond Synperiplanar The Proteolysis Map Thiol Three-center four-electron bond Three-center two-electron bond Threonine Topaquinone Trans isomer Transglutamination Transition state Tryptophan Tryptophan tryptophylquinone Tyrosine Tyrosine sulfation UV Ubiquitination Van der Waals force Water Wavelength

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