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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. 310 helix - Wikipedia

    en.wikipedia.org/wiki/310_helix

    The amino acids in a 3 10-helix are arranged in a right-handed helical structure. Each amino acid corresponds to a 120° turn in the helix (i.e., the helix has three residues per turn), and a translation of 2.0 Å (0.20 nm) along the helical axis, and has 10 atoms in the ring formed by making the hydrogen bond.

  4. Helix - Wikipedia

    en.wikipedia.org/wiki/Helix

    The alpha helix in biology as well as the A and B forms of DNA are also right-handed helices. The Z form of DNA is left-handed. In music , pitch space is often modeled with helices or double helices, most often extending out of a circle such as the circle of fifths , so as to represent octave equivalency .

  5. Protein secondary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_secondary_structure

    These methods were based on the helix- or sheet-forming propensities of individual amino acids, sometimes coupled with rules for estimating the free energy of forming secondary structure elements. The first widely used techniques to predict protein secondary structure from the amino acid sequence were the Chou–Fasman method [ 17 ] [ 18 ] [ 19 ...

  6. Supersecondary structure - Wikipedia

    en.wikipedia.org/wiki/Supersecondary_structure

    When viewed from the N-terminal side of the beta strands, so that one strand is on top of the other, a left-handed beta-alpha-beta motif has the alpha helix on the left side of the beta strands. The more common right-handed motif would have an alpha helix on the right side of the plane containing the beta strands. [4]

  7. Alpha-keratin - Wikipedia

    en.wikipedia.org/wiki/Alpha-keratin

    The molecular structure of alpha-keratin. Disulfide bonds between two alpha-helix keratin. α-keratin is a polypeptide chain, typically high in alanine, leucine, arginine, and cysteine, that forms a right-handed α-helix. [3] [4] Two of these polypeptide chains twist together to form a left-handed helical structure known as a coiled coil.

  8. Mortgage and refinance rates for Jan. 6, 2025: Average rates ...

    www.aol.com/finance/mortgage-and-refinance-rates...

    Average mortgage rates are edging down moderately week over week of Monday, January 6, 2024, though remain at elevated levels for benchmark 30-year and 15-year fixed terms, this despite three back ...

  9. Ramachandran plot - Wikipedia

    en.wikipedia.org/wiki/Ramachandran_plot

    Such a clustering is alternatively described in the ABEGO system, where each letter stands for α (and 3 10) helix, right-handed β sheets (and extended structures), left-handed helixes, left-handed sheets, and finally unplottable cis peptide bonds sometimes seen with proline; it has been used in the classification of motifs [14] and more ...