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  2. Ramachandran plot - Wikipedia

    en.wikipedia.org/wiki/Ramachandran_plot

    The ω angle at the peptide bond is normally 180°, since the partial-double-bond character keeps the peptide bond planar. [3] The figure in the top right shows the allowed φ,ψ backbone conformational regions from the Ramachandran et al. 1963 and 1968 hard-sphere calculations: full radius in solid outline, reduced radius in dashed, and ...

  3. Beta sheet - Wikipedia

    en.wikipedia.org/wiki/Beta_sheet

    The peptide backbone dihedral angles (φ, ψ) are about (–140°, 135°) in antiparallel sheets. In this case, if two atoms C α i and C α j are adjacent in two hydrogen-bonded β-strands, then they form two mutual backbone hydrogen bonds to each other's flanking peptide groups; this is known as a close pair of hydrogen bonds.

  4. Peptide bond - Wikipedia

    en.wikipedia.org/wiki/Peptide_bond

    Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.

  5. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    However, additional molecular interactions may render the amide form less stable; the amino group is expelled instead, resulting in an ester (Ser/Thr) or thioester (Cys) bond in place of the peptide bond. This chemical reaction is called an N-O acyl shift. The ester/thioester bond can be resolved in several ways:

  6. Ribbon diagram - Wikipedia

    en.wikipedia.org/wiki/Ribbon_diagram

    Disulfide bonds Interlocked SS symbol or a zigzag, like a stylized lightning stroke. Prosthetic groups or inhibitors Stick figures, or ball & stick. Metals Spheres. Shading and colour Shading or colour adds dimensionality to the diagram. Generally, the features at the front are the highest in contrast and those towards the back are the lowest.

  7. Alpha sheet - Wikipedia

    en.wikipedia.org/wiki/Alpha_sheet

    Diagram of the hydrogen bonding patterns in the alpha sheet structure. Oxygen atoms are shown in red and nitrogen in blue; dotted lines represent hydrogen bonds. R groups represent the amino acid side chains. A stick representation of a peptide chain in an alpha-sheet configuration.

  8. Peptide - Wikipedia

    en.wikipedia.org/wiki/Peptide

    A neuropeptide is a peptide that is active in association with neural tissue. A lipopeptide is a peptide that has a lipid connected to it, and pepducins are lipopeptides that interact with GPCRs. A peptide hormone is a peptide that acts as a hormone. A proteose is a mixture of peptides produced by the hydrolysis of proteins. The term is ...

  9. Peptidyl transferase center - Wikipedia

    en.wikipedia.org/wiki/Peptidyl_transferase_center

    The peptidyl transferase center (EC 2.3.2.12) is an aminoacyltransferase ribozyme (RNA enzyme) located in the large subunit of the ribosome.It forms peptide bonds between adjacent amino acids during the translation process of protein biosynthesis. [1]