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  2. Alpha helix - Wikipedia

    en.wikipedia.org/wiki/Alpha_helix

    The alpha helix is the most common structural arrangement in the secondary structure of proteins. It is also the most extreme type of local structure, and it is the local structure that is most easily predicted from a sequence of amino acids. The alpha helix has a right-handed helix conformation in which every backbone N−H group hydrogen ...

  3. Helical wheel - Wikipedia

    en.wikipedia.org/wiki/Helical_wheel

    The plot reveals whether hydrophobic amino acids are concentrated on one side of the helix, usually with polar or hydrophilic amino acids on the other. This arrangement is common in alpha helices within globular proteins, where one face of the helix is oriented toward the hydrophobic core and one face is oriented toward the solvent-exposed surface.

  4. List of chemistry mnemonics - Wikipedia

    en.wikipedia.org/wiki/List_of_chemistry_mnemonics

    A mnemonic is a memory aid used to improve long-term memory and make the process of consolidation easier. Many chemistry aspects, rules, names of compounds, sequences of elements, their reactivity, etc., can be easily and efficiently memorized with the help of mnemonics. This article contains the list of certain mnemonics in chemistry.

  5. N cap - Wikipedia

    en.wikipedia.org/wiki/N_cap

    Because of this it is sometimes also described as the residue prior to the helix. Capping motifs are those often found at the N cap. Asx turns, ST turns, and asx motifs are often found at such situations, with the asx or serine or threonine residue at the N cap. The C cap is the corresponding amino acid residue at the other end of the helix

  6. Protein secondary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_secondary_structure

    Proline and glycine are sometimes known as "helix breakers" because they disrupt the regularity of the α helical backbone conformation; however, both have unusual conformational abilities and are commonly found in turns. Amino acids that prefer to adopt helical conformations in proteins include methionine, alanine, leucine, glutamate and ...

  7. Leucine zipper - Wikipedia

    en.wikipedia.org/wiki/Leucine_zipper

    These amino acids are spaced out in each region's polypeptide sequence in such a way that when the sequence is coiled in a 3D alpha-helix, the leucine residues line up on the same side of the helix. This region of the alpha-helix - containing the leucines which line up - is called a ZIP domain, and leucines from each ZIP domain can weakly ...

  8. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    The 21 proteinogenic α-amino acids found in eukaryotes, grouped according to their side chains' pK a values and charges carried at physiological pH (7.4) 2-, alpha-, or α-amino acids [21] have the generic formula H 2 NCHRCOOH in most cases, [b] where R is an organic substituent known as a "side chain". [22]

  9. C cap - Wikipedia

    en.wikipedia.org/wiki/C_cap

    Because of this it is sometimes also described as the residue following the helix. Certain motifs occur commonly at or around the C cap, notably the Schellman loop and the niche (protein structural motif). The N cap is the corresponding amino acid residue at the other end of the helix

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