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  2. Protein structure prediction - Wikipedia

    en.wikipedia.org/wiki/Protein_structure_prediction

    An alpha-helix with hydrogen bonds (yellow dots) 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 ...

  3. Alpha helix - Wikipedia

    en.wikipedia.org/wiki/Alpha_helix

    An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a 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 ...

  4. 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.

  5. Protein secondary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_secondary_structure

    Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. [ 1 ] The two most common secondary structural elements are alpha helices and beta sheets, though beta turns and omega loops occur as well.

  6. 310 helix - Wikipedia

    en.wikipedia.org/wiki/310_helix

    A 310 helix is a type of secondary structure found in proteins and polypeptides. Of the numerous protein secondary structures present, the 3 10 -helix is the fourth most common type observed; following α-helices, β-sheets and reverse turns. 3 10 -helices constitute nearly 10–15% of all helices in protein secondary structures, and are ...

  7. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    A protein is a polyamide. Secondary structure: regularly repeating local structures stabilized by hydrogen bonds. The most common examples are the α-helix, β-sheet and turns. Because secondary structures are local, many regions of different secondary structure can be present in the same protein molecule.

  8. Helix - Wikipedia

    en.wikipedia.org/wiki/Helix

    A helix (/ ˈhiːlɪks /; pl. helices) is a shape like a cylindrical coil spring or the thread of a machine screw. It is a type of smooth space curve with tangent lines at a constant angle to a fixed axis. Helices are important in biology, as the DNA molecule is formed as two intertwined helices, and many proteins have helical substructures ...

  9. Zinc finger - Wikipedia

    en.wikipedia.org/wiki/Zinc_finger

    Zinc fingers were first identified in a study of transcription in the African clawed frog, Xenopus laevis in the laboratory of Aaron Klug.A study of the transcription of a particular RNA sequence revealed that the binding strength of a small transcription factor (transcription factor IIIA; TFIIIA) was due to the presence of zinc-coordinating finger-like structures. [6]