4.3. The peptide bond

The peptide bond

The amino acids are joined to form peptides and proteins by a peptide bond. If the number of amino acids that make up the peptide is less than ten, it is called an oligopeptide, and if it is greater than ten, the peptide is called a polypeptide.

The peptide bond is a bond between the carboxyl group (-COOH) of one amino acid and the amino group (-NH₂) of another amino acid. The peptide bond involves the loss of a water molecule and the formation of a CO-NH covalent bond. It is actually an amide- type covalent bond.

Amide bond

An amide bond is a bond in which an amino group -NH₂ and a carboxyl group -COOH are attached.

Wolfmankurd at the English language Wikipedia [GFDL or CC-BY-SA-3.0], from Wikimedia Commons

Animated image: Peptide bond formation.

In turn, this bond can be hydrolyzed by separating the two amino acids.

The set of two amino acids linked by a peptide bond is called a dipeptide. If it is three amino acids linked by peptide bonds, tripeptide, and so on.

Generically speaking of oligopeptides when it consists of less than ten amino acids and of polypeptides when there is a high number of amino acids.

By Pozitron (Own work) [CC BY-SA 4.0], via Wikimedia Commons

The two ends of a peptide are not equivalent, since it has an N-terminal and a C-terminal end. By convention, the amino terminus is considered the beginning of the peptide chain.

The peptide bond is stabilized because the carbon, oxygen and nitrogen atoms share electrons, which causes two resonant forms to appear and that the bond between carbon and nitrogen has a partial double bond character.

Due to this partial double bond character of the peptide bond, the arrangement in space of the four atoms of the peptide unit and the two alpha carbon atoms is such that they lie in the same plane (peptide plane) with fixed distances and angles; this planar arrangement is rigid. There is only freedom of rotation around the alpha carbons.

The radicals of the amino acids do not participate in the peptide bonds, being arranged up and down, alternately, in the polypeptide,

The main characteristics of the peptide bond are:

It is an amide-type bond between the carboxyl group of one amino acid and the amino of another with the release of a water molecule, but it is shorter than other bonds.
The peptide bond has a partial double bond character, which is why it is rigid and does not show twist, which causes the atoms involved (C and N, as well as O and H) to lie in the same plane.
The peptide bond presents polarity with the appearance of charge densities in O and N. This property is responsible for the appearance of H bonds between peptide bonds, responsible for the secondary structure of proteins.

Fundamental ideas about the peptide bond

The peptide bond is the one that occurs at the junction of two amino acids. The carboxyl group (-COOH) of an amino acid and the amino group (-NH₂) of another amino acid are joined, detaching themselves from a water molecule.

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Skip navigation Biology 2nd Baccalaureate Biology 2nd Bac. 1. Bioelements and biomolecules. Water and mineral salts 1.1. Chemical bonds in biology 1.1.1. Intramolecular bonds 1.1.1.1. Covalent bond 1.1.1.2. Ionic bond 1.1.2. Intermolecular bonds 1.1.2.1. Van der Waals forces 1.1.2.2. Hydrogen bonds 1.2. The chemical basis of life: inorganic and organic components 1.2.1. Primary bioelements 1.2.2. Secondary bioelements 1.2.3. Trace elements 1.3. The immediate principles or biomolecules 1.3.1. Water 1.3.1.1. Chemical structure of water 1.3.1.2. Properties and functions of water 1.3.2. Mineral salts 1.3.2.1. Functions of salts in solution 1.3.2.2. Colloidal solutions and dispersions 1.3.2.3. Properties of colloidal dispersions 1.3.2.4. Diffusion, osmosis and dialysis 1.3.2.4.1. Diffusion 1.3.2.4.2. Osmosis 1.3.2.4.3. Dialysis 1.4. Bibliography 2. Glucides 2.1. Glucid concept 2.2. Classification of carbohydrates 2.3. Monosaccharides 2.3.1. Trioses 2.3.1.1. Spatial isomerism or stereoisomerism 2.3.2. Tetroses 2.3.3. Pentoses 2.3.3.1. Monosaccharide cyclization 2.3.4. Hexoses 2.4. The N-glucosidic and O-glucosidic bonds 2.4.1. Substances derived from monosaccharides 2.5. Disaccharides 2.6. Polysaccharides 2.6.1. Homopolysaccharides 2.6.1.1. Reserve homopolysaccharides 2.6.1.2. Structural homopolysaccharides 2.6.2. Heteropolysaccharides 2.6.3. Heterosides 2.7. General functions of glucides 2.8. Bibliography 3. Lipids 3.1. Lipid concept 3.2. Classification of lipids 3.2.1. Fatty acids 3.2.1.1. Saturated and unsaturated fatty acids 3.2.1.2. Chemical properties of fatty acids 3.2.1.3. Physical properties of fatty acids 3.2.1.4. Fatty Acid Functions 3.2.2. Saponifiable lipids or with fatty acids 3.2.2.1. Simple lipids 3.2.2.1.1. Acylglycerides 3.2.2.1.2. Cerides 3.2.2.2. Complex lipids 3.2.2.2.1. Phospholipids 3.2.2.2.2. Glycolipids 3.2.3. Unsaponifiable lipids or without fatty acids 3.3. Lipid functions 3.4. Bibliography 4. Proteins 4.1. Introduction to proteins 4.2. Amino acids 4.2.1. Classification of amino acids 4.2.2. Properties of amino acids 4.3. The peptide bond 4.4. Protein 4.4.1. Protein structure 4.4.1.1. Primary structure of proteins 4.4.1.2. Secondary structure of proteins 4.4.1.3. Tertiary structure of proteins 4.4.1.4. Quaternary structure of proteins 4.4.2. Protein properties 4.4.3. Classification of proteins 4.4.3.1. Holoproteins 4.4.3.2. Heteroproteins 4.4.4. Protein functions 4.5. Enzymes 4.5.1. Structure of enzymes 4.5.2. The active center of enzymes 4.5.3. General Mechanism of Enzyme Catalysis 4.5.4. Regulation of enzyme activity 4.5.5. Allosteric enzymes 4.5.6. Nomenclature and classification of enzymes 4.6. The vitamins 4.6.1. Fat-soluble vitamins 4.6.2. Water soluble vitamins 4.7. Bibliography 5. Nucleotides and nucleic acids 5.1. The chemical composition of nucleic acids 5.1.1. Components of nucleic acids 5.1.2. Concept, types and functions of nucleic acids 5.1.3. Nucleosides 5.1.4. Nucleotides 5.1.4.1. Nucleotide functions 5.1.5. Nucleic acids 5.2. Deoxyribonucleic acid (DNA) 5.2.1. DNA structure 5.2.1.1. Primary structure of DNA 5.2.1.2. Secondary structure of DNA 5.2.1.3. Tertiary structure of DNA 5.2.1.3.1. Tertiary structure of DNA in prokaryotes 5.2.1.3.2. Tertiary structure of DNA in eukaryotes 5.2.1.4. Quaternary structure of DNA 5.2.2. DNA types 5.2.3. Genetic material: chromatin and chromosomes 5.2.3.1. Karyotype and karyogram 5.3. Ribonucleic acid (RNA) 5.3.1. RNA types 5.3.1.1. Transfer RNA 5.3.1.2. Messenger RNA 5.3.1.3. Ribosomal RNA 5.3.1.4. Nucleolar RNA 5.3.1.5. Small nuclear RNA 5.3.2. Functions of ribonucleic acids 5.4. Bibliography 6. Cell morphology 6.1. Cell concept 6.1.1. Cell history 6.1.2. Cell theory 6.2. Levels of cellular organization 6.2.1. General characteristics of cells 6.2.2. Prokaryotic cells 6.2.2.1. Prokaryotic cell morphology 6.2.2.2. Structure of prokaryotes 6.2.2.2.1. Bacterial capsule 6.2.2.2.2. Bacterial wall 6.2.2.2.3. Plasma membrane 6.2.2.2.4. Cytoplasm-Ribosomes-Inclusions 6.2.2.2.5. Bacterial DNA 6.2.2.2.6. Bacterial appendages 6.2.2.3. Bacteria Physiology 6.2.3. Eukaryotic cells 6.2.3.1. Animal and plant cell 6.2.3.1.1. Animal eukaryotic cell 6.2.3.1.2. Plant eukaryotic cell 6.2.3.2. Cell Evolution: Endosymbiont Theory 6.3. Size, shape and quantity 6.4. The plasma membrane 6.4.1. Chemical composition of the membrane 6.4.2. The structure of the membrane. The fluid mosaic model 6.4.3. Functions of the plasma membrane 6.4.4. Transport across the membrane 6.4.4.1. Small molecule transport 6.4.4.2. Macromolecule transport 6.4.5. Plasma membrane differentiations 6.5. The cell wall of plant cells 6.5.1. Chemical composition of the cell wall 6.5.2. Cell wall structure 6.5.3. Cell wall differentiations 6.5.4. Cell wall functions 6.6. Extracellular matrix or glucocalyx 6.7. Cytosol or hyaloplasm 6.8. The cytoskeleton 6.8.1. Microfilaments or actin filaments 6.8.2. Intermediate filaments 6.8.3. Microtubules 6.9. Cell membrane and organelle systems 6.9.1. Membrane systems 6.9.1.1. The endoplasmic reticulum 6.9.1.2. Golgi apparatus 6.9.2. Cell organelles 6.9.2.1. Lysosomes 6.9.2.2. Peroxisomes 6.9.2.3. Vacuoles 6.9.2.4. Mitochondria 6.9.2.4.1. Functions of the mitochondria 6.9.2.5. Plastids 6.9.2.5.1. Chloroplasts 6.9.2.6. Ribosomes 6.9.2.7. Centrosome 6.9.2.8. Cilia and flagella 6.10. Cell motility 6.11. The cell nucleus 6.11.1. Characteristics of the cell nucleus 6.11.2. The interphase nucleus 6.11.3. The mitotic nucleus or nucleus in division 6.12. Bibliography 7. Metabolism 7.1. Metabolism 7.1.1. Energetic Aspects of Cellular Chemical Reactions 7.2. Catabolism 7.2.1. Catabolism and obtaining energy 7.2.2. Carbohydrate catabolism 7.2.2.1. Glycolysis 7.2.2.2. Cellular respiration 7.2.2.2.1. Oxidative decarboxylation 7.2.2.2.2. Krebs cycle 7.2.2.2.3. Electron transport chain 7.2.2.2.4. Energy balance of cellular respiration 7.2.2.3. Fermentations 7.2.2.3.1. Alcoholic or ethyl fermentation 7.2.2.3.2. Lactic fermentation 7.2.2.3.3. Other types of fermentations 7.3. Anabolism 7.3.1. Autotrophic anabolism 7.3.2. Photosynthesis 7.3.2.1. Photochemical or light phase 7.3.2.1.1. Photosystems 7.3.2.1.2. Photophosphorylation 7.3.2.1.2.1. Non cyclic photophosphorylation 7.3.2.1.2.2. Cyclic photophosphorylation 7.3.2.2. Biosynthetic or dark phase 7.3.2.3. Factors influencing photosynthesis 7.3.2.4. Products of photosynthesis 7.3.3. Chemosynthesis 7.4. Bibliography 8. Cell reproduction 8.1. The cell cycle 8.1.1. Interphase 8.1.2. Cellular division 8.2. Cellular division 8.2.1. Mitosis 8.2.1.1. Prophase 8.2.1.2. Metaphase 8.2.1.3. Anaphase 8.2.1.4. Telophase 8.2.1.5. Cytokinesis 8.2.1.6. More on mitosis 8.2.2. Meiosis 8.2.2.1. Meiosis I 8.2.2.2. Meiosis II 8.2.3. Meiosis and sexual reproduction 8.2.4. Meiosis and life cycle 8.2.5. Biological importance of meiosis 8.3. Differences and similarities between mitosis and meiosis 8.4. Bibliography 9. Classical genetics 9.1. Genetics basics 9.2. Mendelian genetics 9.2.1. The method 9.2.2. Mendel's Laws 9.2.2.1. Mendel's first law or principle of uniformity in the first generation 9.2.2.2. Mendel's second law or principle of segregation 9.2.2.2.1. Backcross and test crossover 9.2.2.3. Mendel's third law or principle of independent combination 9.3. Gene interaction 9.3.1. Gene interaction between allelic genes 9.3.2. Gene interaction between non-allelic genes that influence for the same trait 9.4. Chromosomal theory of heredity 9.5. Ligation and recombination 9.6. Complex mendelism 9.6.1. Multiple allelism 9.6.1.1. Lethal genes 9.6.2. Pleiotropy 9.6.3. Expressiveness and genetic penetrance 9.7. Sex-linked inheritance 9.7.1. Y-linked inheritance 9.7.2. X-linked inheritance 9.8. Heredity influenced by sex 9.9. Bibliography 10. Molecular genetics 10.1. DNA as hereditary material 10.2. DNA replication 10.2.1. The need for DNA replication 10.2.2. First hypotheses about DNA duplication 10.2.3. Meselson and Stahl experiment 10.2.4. The sense of growth of the new strands 10.2.5. Mechanism of DNA replication 10.2.5.1. Replication in prokaryotes 10.2.5.2. Replication in eukaryotes 10.2.6. Error correction 10.2.7. Enzymes involved in replication 10.3. Gene concept 10.4. "One gene-one enzyme" theory 10.5. Transcription 10.5.1. Mechanism of transcription 10.5.1.1. Transcription in prokaryotes 10.5.1.2. Eukaryotic transcription 10.6. Translation or protein biosynthesis 10.6.1. The genetic code 10.6.2. Mechanism of translation of RNA to proteins 10.6.2.1. Translation in eukaryotes 10.7. Regulation of gene expression 10.8. Bibliography 11. Genetics and evolution 11.1. Mutations 11.2. Types of mutations 11.2.1. Gene or point mutation 11.2.2. Chromosomal or structural mutation 11.2.3. Mutation at the genomic level 11.3. Causes of mutations 11.4. Evolutionary implications of mutations 11.5. Metabolic implications of mutations 11.6. Bibliography 12. Microbiology and biotechnology 12.1. Microbiology 12.2. Viruses 12.2.1. Viral morphology 12.2.2. Viral physiology 12.2.2.1. Lytic cycle 12.2.2.2. Lysogenic cycle 12.2.2.3. Cycles of viruses of special interest 12.2.2.3.1. Flu virus life cycle 12.2.2.3.2. Life cycle of the AIDS virus 12.3. Other acellular forms 12.3.1. Viroids 12.3.2. Prions 12.4. Biotechnology 12.5. Bibliography 13. Immunology 13.1. Infection concept 13.2. Defense mechanisms against infections 13.2.1. Nonspecific mechanisms 13.2.1.1. Primary barriers: external defenses 13.2.1.2. Secondary barriers: internal defenses 13.2.2. Specific mechanisms 13.3. Immunity and immune system 13.3.1. Components of the immune system 13.3.2. Concept and nature of antigens 13.4. The immune response 13.4.1. Humoral immune response: the antibodies 13.4.1.1. Antibody-producing cells: B lymphocytes 13.4.1.2. Antibodies 13.4.1.2.1. Types of antibodies 13.4.1.2.2. Antigen-antibody reaction 13.4.1.3. Immune memory: primary and secondary responses 13.4.2. Cellular immune response: T lymphocytes 13.5. Types of immunity 13.5.1. Natural immunity 13.5.2. Artificial immunity 13.6. Immune system disorders 13.6.1. Autoimmunity 13.6.2. Hypersensitivity 13.6.3. Immunodeficiency 13.6.4. Transplants and the phenomenon of rejections 13.7. Bibliography « Previous \| Next » 4.3. The peptide bond The peptide bond The amino acids are joined to form peptides and proteins by a *peptide bond. If the number of amino acids that make up the peptide is less than ten, it is called an oligopeptide,* and if it is greater than ten, the peptide is called a polypeptide. The peptide bond is a bond between the carboxyl group (-COOH) of one amino acid and the amino group (-NH₂) of another amino acid. The peptide bond involves the loss of a water molecule and the formation of a CO-NH covalent bond. It is actually an amide- type covalent bond. Amide bond An amide bond is a bond in which an amino group -NH₂ and a carboxyl group -COOH are attached. Wolfmankurd at the English language Wikipedia [GFDL or CC-BY-SA-3.0], from Wikimedia Commons Animated image: Peptide bond formation. In turn, this bond can be hydrolyzed by separating the two amino acids. The set of two amino acids linked by a peptide bond is called a dipeptide. If it is three amino acids linked by peptide bonds, tripeptide, and so on. Generically speaking of oligopeptides when it consists of less than ten amino acids and of polypeptides when there is a high number of amino acids. By Pozitron (Own work) [CC BY-SA 4.0], via Wikimedia Commons The two ends of a peptide are not equivalent, since it has an N-terminal and a C-terminal end. By convention, the amino terminus is considered the beginning of the peptide chain. The peptide bond is stabilized because the carbon, oxygen and nitrogen atoms share electrons, which causes two resonant forms to appear and that the bond between carbon and nitrogen has a partial double bond character. Due to this partial double bond character of the peptide bond, the arrangement in space of the four atoms of the peptide unit and the two alpha carbon atoms is such that they lie in the same plane (peptide plane) with fixed distances and angles; this planar arrangement is rigid. There is only freedom of rotation around the alpha carbons. The radicals of the amino acids do not participate in the peptide bonds, being arranged up and down, alternately, in the polypeptide, The main characteristics of the peptide bond are: It is an amide-type bond between the carboxyl group of one amino acid and the amino of another with the release of a water molecule, but it is shorter than other bonds. The peptide bond has a partial double bond character, which is why it is rigid and does not show twist, which causes the atoms involved (C and N, as well as O and H) to lie in the same plane. The peptide bond presents polarity with the appearance of charge densities in O and N. This property is responsible for the appearance of H bonds between peptide bonds, responsible for the secondary structure of proteins. Fundamental ideas about the peptide bond The peptide bond is the one that occurs at the junction of two amino acids. The carboxyl group (-COOH) of an amino acid and the amino group (-NH₂) of another amino acid are joined, detaching themselves from a water molecule. Licensed under the Creative Commons Attribution Share Alike License 4.0 « Previous \| Next » These pages are semi-automatically translated from the web Biology 2nd Baccalaureate. Biología de 2º de Bachillerato (biologia-geologia.com). 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The peptide bond