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General scheme for RiPP biosynthesis. All RiPPs are synthesized first at the ribosome as a precursor peptide . This peptide consists of a core peptide segment which is typically preceded (and occasionally followed) by a leader peptide segment and is typically ~20-110 residues long.
Secondary cloverleaf structure of tRNA Phe from yeast.. The cloverleaf model of tRNA is a model that depicts the molecular structure of tRNA. [1] The model revealed that the chain of tRNA consists of two ends—sometimes called "business ends"—and three arms.
Radical S-Adenosylmethionine (SAM) Enzymes in Cofactor Biosynthesis: A Treasure Trove of Complex Organic Radical Rearrangement Reactions: [12] Molecular architectures and functions of radical enzymes and their (re)activating proteins: [13] Radical SAM enzymes in RiPP biosynthesis. [14] Radical SAM enzymes with a vitamin B 12 (cobalamin)-binding ...
Hydroxyproline is a major component of the protein collagen, [3] comprising roughly 13.5% of mammalian collagen. Hydroxyproline and proline play key roles for collagen stability. [4] They permit the sharp twisting of the collagen helix. [5]
Type III collagen is synthesized by cells as a pre-procollagen. [6] The signal peptide is cleaved off producing a procollagen molecule. Three identical type III procollagen chains come together at the carboxy-terminal ends, and the structure is stabilized by the formation of disulphide bonds. Each individual chain folds into a left-handed helix ...
Plant development: AtAGP19: Stem, flower, root and leaf Cell division and expansion, leaf development and reproduction [106] AtAGP57C: Rosette leaf, silique, seed, flower, and shoot apex of inflorescence stem Cell wall structure maintenance [107] AtFLA1: Stomata, trichome, leaf vasculature, primary root tip and lateral root
Collagen IV (ColIV or Col4) is a type of collagen found primarily in the basal lamina. The collagen IV C4 domain at the C-terminus is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel. Also, collagen IV lacks the regular glycine in every third residue necessary for the tight, collagen helix ...
Plant lipid transfer proteins consist of 4 alpha-helices in a right-handed superhelix with a folded leaf topology. The structure is stabilised by disulfide bridges linking the helices to each other. The structure forms an internal hydrophobic cavity in which 1-2 lipids can be bound.