A report on Amino acid

Structure of a generic L-amino acid in the "neutral" form needed for defining a systematic name, without implying that this form actually exists in detectable amounts either in aqueous solution or in the solid state.

The 21 proteinogenic α-amino acids found in eukaryotes, grouped according to their side chains' pKa values and charges carried at physiological pH (7.4)

Ionization and Brønsted character of N-terminal amino, C-terminal carboxylate, and side chains of amino acid residues

Composite of titration curves of twenty proteinogenic amino acids grouped by side chain category

Share of amino acid in various human diets and the resulting mix of amino acids in human blood serum. Glutamate and glutamine are the most frequent in food at over 10%, while alanine, glutamine, and glycine are the most common in blood.

The condensation of two amino acids to form a dipeptide. The two amino acid residues are linked through a peptide bond

Catabolism of proteinogenic amino acids. Amino acids can be classified according to the properties of their main degradation products:
* Glucogenic, with the products having the ability to form glucose by gluconeogenesis
* Ketogenic, with the products not having the ability to form glucose. These products may still be used for ketogenesis or lipid synthesis.
* Amino acids catabolized into both glucogenic and ketogenic products.

Amino acids are organic compounds that contain amino (\sNH3+) and carboxylic acid (\sCO2H) functional groups, along with a side chain (R group) specific to each amino acid.

- Amino acid

131 related topics with Alpha

Protein

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John Kendrew with model of myoglobin in progress

Chemical structure of the peptide bond (bottom) and the three-dimensional structure of a peptide bond between an alanine and an adjacent amino acid (top/inset). The bond itself is made of the CHON elements.

Resonance structures of the peptide bond that links individual amino acids to form a protein polymer

A ribosome produces a protein using mRNA as template

The DNA sequence of a gene encodes the amino acid sequence of a protein

The crystal structure of the chaperonin, a huge protein complex. A single protein subunit is highlighted. Chaperonins assist protein folding.

Three possible representations of the three-dimensional structure of the protein triose phosphate isomerase. Left: All-atom representation colored by atom type. Middle: Simplified representation illustrating the backbone conformation, colored by secondary structure. Right: Solvent-accessible surface representation colored by residue type (acidic residues red, basic residues blue, polar residues green, nonpolar residues white).

Molecular surface of several proteins showing their comparative sizes. From left to right are: immunoglobulin G (IgG, an antibody), hemoglobin, insulin (a hormone), adenylate kinase (an enzyme), and glutamine synthetase (an enzyme).

The enzyme hexokinase is shown as a conventional ball-and-stick molecular model. To scale in the top right-hand corner are two of its substrates, ATP and glucose.

Ribbon diagram of a mouse antibody against cholera that binds a carbohydrate antigen

Proteins in different cellular compartments and structures tagged with green fluorescent protein (here, white)

Constituent amino-acids can be analyzed to predict secondary, tertiary and quaternary protein structure, in this case hemoglobin containing heme units

Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues.

Essential amino acid

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An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized from scratch by the organism fast enough to supply its demand, and must therefore come from the diet.

Biosynthesis

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Multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms.

Uridine monophosphate (UMP) biosynthesis

'Thymidylate synthase reaction: dUMP + 5,10-methylenetetrahydrofolate ⇔ dTMP + dihydrofolate

Ctp synthase mechanism: UTP + ATP + glutamine ⇔ CTP + ADP + glutamate

As DNA polymerase moves in a 3' to 5' direction along the template strand, it synthesizes a new strand in the 5' to 3' direction

Glutamine oxoglutarate aminotransferase and glutamine synthetase

The diaminopimelic acid lysine biosynthetic pathway

The tRNA anticodon interacts with the mRNA codon in order to bind an amino acid to growing polypeptide chain.

Familial hypercholesterolemia causes cholesterol deposits

Some important biological macromolecules include: proteins, which are composed of amino acid monomers joined via peptide bonds, and DNA molecules, which are composed of nucleotides joined via phosphodiester bonds.

Neurotransmitter

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Signaling molecule secreted by a neuron to affect another cell across a synapse.

Acetylcholine is cleaved in the synaptic cleft into acetic acid and choline

CAPON Binds Nitric Oxide Synthase, Regulating NMDA Receptor–Mediated Glutamate Neurotransmission

Many neurotransmitters are synthesized from simple and plentiful precursors such as amino acids, which are readily available and often require a small number of biosynthetic steps for conversion.

Methionine

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Essential amino acid in humans.

Methionine (abbreviated as Met or M; encoded by the codon AUG) is an α-amino acid that is used in the biosynthesis of proteins.

Nitrogen

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Chemical element with the symbol N and atomic number 7.

The shapes of the five orbitals occupied in nitrogen. The two colours show the phase or sign of the wave function in each region. From left to right: 1s, 2s (cutaway to show internal structure), 2px, 2py, 2pz.

Table of nuclides (Segrè chart) from carbon to fluorine (including nitrogen). Orange indicates proton emission (nuclides outside the proton drip line); pink for positron emission (inverse beta decay); black for stable nuclides; blue for electron emission (beta decay); and violet for neutron emission (nuclides outside the neutron drip line). Proton number increases going up the vertical axis and neutron number going to the right on the horizontal axis.

Molecular orbital diagram of dinitrogen molecule, N2. There are five bonding orbitals and two antibonding orbitals (marked with an asterisk; orbitals involving the inner 1s electrons not shown), giving a total bond order of three.

Solid nitrogen on the plains of Sputnik Planitia on Pluto next to water ice mountains

Structure of [Ru(NH3)5(N2)]2+ (pentaamine(dinitrogen)ruthenium(II)), the first dinitrogen complex to be discovered

Mesomeric structures of borazine, (–BH–NH–)3

Standard reduction potentials for nitrogen-containing species. Top diagram shows potentials at pH 0; bottom diagram shows potentials at pH 14.

Nitrogen dioxide at −196 °C, 0 °C, 23 °C, 35 °C, and 50 °C. converts to colourless dinitrogen tetroxide at low temperatures, and reverts to at higher temperatures.

Fuming nitric acid contaminated with yellow nitrogen dioxide

Schematic representation of the flow of nitrogen compounds through a land environment

A container vehicle carrying liquid nitrogen.

Nitrogen occurs in all organisms, primarily in amino acids (and thus proteins), in the nucleic acids (DNA and RNA) and in the energy transfer molecule adenosine triphosphate.

This process uses transfer RNA (tRNA) molecules to deliver amino acids to the ribosome, where ribosomal RNA (rRNA) then links amino acids together to form coded proteins.