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  2. Beta turn - Wikipedia

    en.wikipedia.org/wiki/Beta_turn

    Apart from the type I, I’,II and II’ beta turns as identified via the hydrogen bond criterion, non-hydrogen-bonded beta-turns named type VIII often occur. Three other, fairly rare, types of beta turn have been identified in which the peptide bond between residues i+1 and i+2 is cis rather than trans; these are named types VIa1, VIa2 and VIb ...

  3. Turn (biochemistry) - Wikipedia

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

    Over the years, many beta turn prediction methods have been developed. Recently, Dr. Raghava's Group developed BetaTPred3 method which predicts a complete beta turn rather than individual residues falling into a beta turn. The method also achieves good accuracy and is the first method which predicts all 9 types of beta turns.

  4. Beta bend ribbon - Wikipedia

    en.wikipedia.org/wiki/Beta_bend_ribbon

    Beta bend ribbons may be formed from any of these types but type I is the commonest in proteins, as it is for single beta turns. Beta bend ribbons made from type I or I’ turns are somewhat twisted, while beta bend ribbons made from type II or II’ beta turns are flat. Beta bend ribbons with mixtures of different beta turn types also occur.

  5. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    The formation of a peptide bond requires an input of energy. The two reacting molecules are the alpha amino group of one amino acid and the alpha carboxyl group of the other amino acids. A by-product of this bond formation is the release of water (the amino group donates a proton while the carboxyl group donates a hydroxyl).

  6. Protein secondary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_secondary_structure

    The two most common secondary structural elements are alpha helices and beta sheets, though beta turns and omega loops occur as well. Secondary structure elements typically spontaneously form as an intermediate before the protein folds into its three dimensional tertiary structure.

  7. Protein catabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_catabolism

    In molecular biology, protein catabolism is the breakdown of proteins into smaller peptides and ultimately into amino acids. Protein catabolism is a key function of digestion process. Protein catabolism often begins with pepsin, which converts proteins into polypeptides. These polypeptides are then further degraded.

  8. Beta-peptide - Wikipedia

    en.wikipedia.org/wiki/Beta-peptide

    β-alanine, an example of a β-amino acid. The amino group attaches not to the α carbon but to the β-carbon, which in this case is a methylene group.. Beta-peptides (β-peptides) are peptides derived from β-amino acids, in which the amino group is attached to the β-carbon (i.e. the carbon two atoms away from the carboxylate group).

  9. Cell signaling - Wikipedia

    en.wikipedia.org/wiki/Cell_signaling

    Biochemical changes can reduce receptor affinity for a ligand. [41] Reducing the sensitivity of the receptor is a result of receptors being occupied for a long time. This results in a receptor adaptation in which the receptor no longer responds to the signaling molecule. Many receptors have the ability to change in response to ligand ...