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(biochemistry) A nonessential amino acid C <sub>5</sub> H <sub>9</sub> NO <sub>2</sub> found in most animal proteins, especially collagen; its cyclic structure leads to kinks in the peptide chain of proteins.
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It possesses an amino N-terminal Src-homology 3 domain (SH3) domain, followed by a proline-rich domain (PRR) and a substrate domain (SD).
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The reaction taking place is between a simple aldehyde, such as propionaldehyde, and an imine derived from ethyl glyoxylate and p-methoxyaniline (PMP = paramethoxphenyl) catalyzed by (S)-proline in dioxane at room temperature.
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The acidity of the phagolysosome is essential for C.burnetii to transport glucose, glutamate, and proline, as well as for its synthesis of nucleic acids and proteins.
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Combined with isotopic labelling evidence and computational studies, the proposed reaction mechanism for proline-catalyzed aldol reactions is as follows: This strategy allows the otherwise challenging cross-aldol reaction between two aldehydes.
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The enantioselectivity is further controlled by hydrogen bonding between the proline carboxylic acid group and the imine.
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The Ser residue is generally in the sequence -Ser-Gly-X-Gly- (where X can be any amino acid residue but proline), although not every protein with this sequence has an attached glycosaminoglycan.
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Under the Hajos-Parrish conditions only a catalytic amount of proline is necessary (3 mol%).
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These proline-rich stretches are characteristic of SH3-binding sites.
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While traditional synthetic methods accomplish the synthesis of hexoses using variations of iterative protection-deprotection strategies, requiring 8–14 steps, organocatalysis can access many of the same substrates using an efficient two-step protocol involving the proline-catalyzed dimerization of alpha-oxyaldehydes followed by tandem Mukaiyama aldol cyclization.
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Proline-catalyzed aldol reactions do not show any non-linear effects (the enantioselectivity of the products is directly proportional to the enantiopurity of the catalyst).
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More specifically the I-band contains two regions of tandem type II immunoglobulin domains on either side of a PEVK region which is rich in proline (P), glutamate (E), valine (V) and lysine (K).
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In a seminal example, proline efficiently catalyzed the cyclization of a triketone: This reaction is known as the Hajos-Parrish reaction (also known as the Hajos-Parrish-Eder-Sauer-Wiechert reaction, referring to a contemporaneous report from Schering of the reaction under harsher conditions).
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Within the gene are found a large number of PEVK (proline-glutamate-valine-lysine -abundant structural motifs) exons 84 to 99 nucleotides in length which code for conserved 28- to 33-residue motifs which may represent structural units of the titin PEVK spring.
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The most frequently hydroxylated residue in human proteins is proline.
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In some cases, proline may be hydroxylated instead on its β-C atom.
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15 sinne gevind in 4 ms. Hulle kom uit baie bronne en word nie nagegaan nie.