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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 anatomy mnemonics - Wikipedia

    en.wikipedia.org/wiki/List_of_anatomy_mnemonics

    This is a list of human anatomy mnemonics, categorized and alphabetized.For mnemonics in other medical specialties, see this list of medical mnemonics.Mnemonics serve as a systematic method for remembrance of functionally or systemically related items within regions of larger fields of study, such as those found in the study of specific areas of human anatomy, such as the bones in the hand ...

  5. List of medical mnemonics - Wikipedia

    en.wikipedia.org/wiki/List_of_medical_mnemonics

    This is a list of mnemonics used in medicine and medical science, categorized and alphabetized. A mnemonic is any technique that assists the human memory with information retention or retrieval by making abstract or impersonal information more accessible and meaningful, and therefore easier to remember; many of them are acronyms or initialisms which reduce a lengthy set of terms to a single ...

  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. 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

  8. 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 ...

  9. Asparagine - Wikipedia

    en.wikipedia.org/wiki/Asparagine

    Asparagine (symbol Asn or N [2]) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH + 3 form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side chain carboxamide ...