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  2. Structural motif - Wikipedia

    en.wikipedia.org/wiki/Structural_motif

    The structure is also known as a hairpin or hairpin loop. It occurs when two regions of the same strand, usually complementary in nucleotide sequence when read in opposite directions, base-pair to form a double helix that ends in an unpaired loop. The resulting structure is a key building block of many RNA secondary structures. Cruciform DNA

  3. Coiled coil - Wikipedia

    en.wikipedia.org/wiki/Coiled_coil

    Secondary and tertiary structure of the coiled-coil motif. The heptad repeat often consists of specific amino acids, seen in the figure. Knobs into packing is also shown. [27] The general problem of deciding on the folded structure of a protein when given the amino acid sequence (the so-called protein folding problem) has only been solved ...

  4. Rossmann fold - Wikipedia

    en.wikipedia.org/wiki/Rossmann_fold

    Phylogenetic analysis of the NADP binding enzyme adrenodoxin reductase revealed that from prokaryotes, through metazoa and up to primates the sequence motif difference from that of most FAD and NAD-binding sites is strictly conserved. [13] In many articles and textbooks, a Rossmann fold is defined as a strict repeated series of βαβ structure.

  5. Leucine zipper - Wikipedia

    en.wikipedia.org/wiki/Leucine_zipper

    "Overhead view", or helical wheel diagram, of a leucine zipper, where d represents leucine, arranged with other amino acids on two parallel alpha helices.. A leucine zipper (or leucine scissors [1]) is a common three-dimensional structural motif in proteins.

  6. Sequence motif - Wikipedia

    en.wikipedia.org/wiki/Sequence_motif

    In biology, a sequence motif is a nucleotide or amino-acid sequence pattern that is widespread and usually assumed to be related to biological function of the macromolecule. For example, an N -glycosylation site motif can be defined as Asn, followed by anything but Pro, followed by either Ser or Thr, followed by anything but Pro residue .

  7. Zinc finger - Wikipedia

    en.wikipedia.org/wiki/Zinc_finger

    A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn 2+) which stabilizes the fold. It was originally coined to describe the finger-like appearance of a hypothesized structure from the African clawed frog (Xenopus laevis) transcription factor IIIA.

  8. Structural bioinformatics - Wikipedia

    en.wikipedia.org/wiki/Structural_bioinformatics

    Three-dimensional structure of a protein. Structural bioinformatics is the branch of bioinformatics that is related to the analysis and prediction of the three-dimensional structure of biological macromolecules such as proteins, RNA, and DNA. It deals with generalizations about macromolecular 3D structures such as comparisons of overall folds ...

  9. Turn (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Turn_(biochemistry)

    According to one definition, a turn is a structural motif where the C α atoms of two residues separated by a few (usually 1 to 5) peptide bonds are close (less than 7 Å [0.70 nm]). [1] The proximity of the terminal C α atoms often correlates with formation of an inter main chain hydrogen bond between the corresponding residues. Such hydrogen ...