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  2. Beta turn - Wikipedia

    en.wikipedia.org/wiki/Beta_turn

    The main chain–main chain hydrogen bond is replaced by a side chain–main chain hydrogen bond. 3D computer superimposition shows that, in proteins, they occur [12] as one of the same four types that beta turns do, except that their relative frequency of occurrence differs: type II’ is the most common, followed by types I, II and I’.

  3. Beta sheet - Wikipedia

    en.wikipedia.org/wiki/Beta_sheet

    Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation .

  4. Turn (biochemistry) - Wikipedia

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

    For example, a beta hairpin connects two hydrogen-bonded, antiparallel β-strands (a rather confusing name, since a β-hairpin may contain many types of turns – α, β, γ, etc.). Beta hairpins may be classified according to the number of residues that make up the turn - that is, that are not part of the flanking β-strands. [7]

  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. Protein fold class - Wikipedia

    en.wikipedia.org/wiki/Protein_fold_class

    All-β proteins are a class of structural domains in which the secondary structure is composed entirely of β-sheets, with the possible exception of a few isolated α-helices on the periphery.

  7. Beta bulge - Wikipedia

    en.wikipedia.org/wiki/Beta_bulge

    The other type is the G1 beta bulge, of which there are two common sorts, both mainly occurring in association with antiparallel sheet; one residue has the α L conformation and is usually a glycine. In one sort, the beta bulge loop , one of the hydrogen bonds of the beta-bulge also forms a beta turn or alpha turn, such that the motif is often ...

  8. DNA clamp - Wikipedia

    en.wikipedia.org/wiki/DNA_clamp

    The beta subunits in turn bind the αε polymerase complex. The α subunit possesses DNA polymerase activity and the ε subunit is a 3’-5’ exonuclease. [9] The beta chain of bacterial DNA polymerase III is composed of three topologically equivalent domains (N-terminal, central, and C-terminal). Two beta chain molecules are tightly ...

  9. Beta scission - Wikipedia

    en.wikipedia.org/wiki/Beta_scission

    Beta scission is an important reaction in the chemistry of thermal cracking of hydrocarbons and the formation of free radicals. Free radicals are formed upon splitting the carbon-carbon bond . Free radicals are extremely reactive and short-lived.