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  2. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Amino acid. Structure of a typical L -alpha-amino acid in the "neutral" form. Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2]

  3. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein structure is the three-dimensional arrangement of atoms in an amino acid -chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer.

  4. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the ...

  5. List of chemistry mnemonics - Wikipedia

    en.wikipedia.org/wiki/List_of_chemistry_mnemonics

    The four most common elements in living organisms – carbon, hydrogen, oxygen, and nitrogen – may be remembered with the acronym CHON. To remember the elements necessary for agriculture; C arbon, H ydrogen, Ca lcium, Iron (Fe), Magnesium (Mg), Manganese (Mn), Copper (Cu), Mo lybdenum, Chlorine (Cl), B oron.

  6. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    The side chains of the standard amino acids, detailed in the list of standard amino acids, have a great variety of chemical structures and properties; it is the combined effect of all of the amino acid side chains in a protein that ultimately determines its three-dimensional structure and its chemical reactivity. [29]

  7. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Protein folding. Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional.

  8. Protein structure prediction - Wikipedia

    en.wikipedia.org/wiki/Protein_structure_prediction

    The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns). The alignment of the H-bonds creates a dipole moment for the helix with a ...

  9. Peptide - Wikipedia

    en.wikipedia.org/wiki/Peptide

    Peptides are short chains of amino acids linked by peptide bonds. [1][2] A polypeptide is a longer, continuous, unbranched peptide chain. [3] Polypeptides that have a molecular mass of 10,000 Da or more are called proteins. [4] Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides.