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  2. Polyproline helix - Wikipedia

    en.wikipedia.org/wiki/Polyproline_helix

    A polyproline helix is a type of protein secondary structure which occurs in proteins comprising repeating proline residues. [1] A left-handed polyproline II helix (PPII, poly-Pro II, κ-helix [2]) is formed when sequential residues all adopt (φ,ψ) backbone dihedral angles of roughly (-75°, 150°) and have trans isomers of their peptide bonds.

  3. Tuftsin - Wikipedia

    en.wikipedia.org/wiki/Tuftsin

    Tyr-Lys-Pro exert considerable regulatory effect on several macrophage functions including: phagocytosis, cell locomotion, superoxide anion production, IgE-dependent cellular cytotoxicity, β-glycuronidase release, and IL-1 production. [2] Selank is an elongated version of tuftsin with a Pro-Gly-Pro appended, i.e. Thr-Lys-Pro-Arg-Pro-Gly-Pro ...

  4. Proline - Wikipedia

    en.wikipedia.org/wiki/Proline

    Peptide bond formation with incoming Pro-tRNA Pro in the ribosome is considerably slower than with any other tRNAs, which is a general feature of N-alkylamino acids. [17] Peptide bond formation is also slow between an incoming tRNA and a chain ending in proline; with the creation of proline-proline bonds slowest of all. [18]

  5. Collagen helix - Wikipedia

    en.wikipedia.org/wiki/Collagen_helix

    In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data. It consists of a triple helix made of the repetitious amino acid sequence glycine-X-Y, where X and Y are frequently proline or hydroxyproline. [2] [3] Collagen folded into a triple helix is known as tropocollagen.

  6. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    This is caused by R-group interactions such as ionic and hydrogen bonds, disulphide bridges, and hydrophobic & hydrophilic interactions. Protein tertiary structure is the three-dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains.

  7. Molecular geometry - Wikipedia

    en.wikipedia.org/wiki/Molecular_geometry

    Molecular geometries can be specified in terms of 'bond lengths', 'bond angles' and 'torsional angles'. The bond length is defined to be the average distance between the nuclei of two atoms bonded together in any given molecule. A bond angle is the angle formed between three atoms across at least two bonds.

  8. Three-center two-electron bond - Wikipedia

    en.wikipedia.org/wiki/Three-center_two-electron_bond

    In many common bonds of this type, the bonding orbital is shifted towards two of the three atoms instead of being spread equally among all three. Example molecules with 3c–2e bonds are the trihydrogen cation (H + 3) and diborane (B 2 H 6). In these two structures, the three atoms in each 3c-2e bond form an angular geometry, leading to a bent ...

  9. Three-center four-electron bond - Wikipedia

    en.wikipedia.org/.../Three-center_four-electron_bond

    3, X = F, Br, Cl, I) via a molecular orbital (MO) description, building on the concept of the "half-bond" introduced by Rundle in 1947. [ 4 ] [ 5 ] In this model, two of the four electrons occupy an all in-phase bonding MO, while the other two occupy a non-bonding MO, leading to an overall bond order of 0.5 between adjacent atoms (see Molecular ...